Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide to water, while oxidizing various organic and inorganic compounds, playing crucial roles in diverse biological processes including stress response, immune defense, and biosynthetic reactions.
An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.
An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC 1.11.1.9.
A hemeprotein from leukocytes. Deficiency of this enzyme leads to a hereditary disorder coupled with disseminated moniliasis. It catalyzes the conversion of a donor and peroxide to an oxidized donor and water. EC 1.11.1.7.
A hemeprotein which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. EC 1.11.1.5.
Peroxidases that utilize ASCORBIC ACID as an electron donor to reduce HYDROGEN PEROXIDE to WATER. The reaction results in the production of monodehydroascorbic acid and DEHYDROASCORBIC ACID.
A 66-kDa peroxidase found in EOSINOPHIL granules. Eosinophil peroxidase is a cationic protein with a pI of 10.8 and is comprised of a heavy chain subunit and a light chain subunit. It possesses cytotoxic activity towards BACTERIA and other organisms, which is attributed to its peroxidase activity.
A hemeprotein that catalyzes the oxidation of the iodide radical to iodine with the subsequent iodination of many organic compounds, particularly proteins. EC 1.11.1.8.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
An agent thought to have disinfectant properties and used as an expectorant. (From Martindale, The Extra Pharmacopoeia, 30th ed, p747)
An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA.
An element with the atomic symbol Se, atomic number 34, and atomic weight 78.96. It is an essential micronutrient for mammals and other animals but is toxic in large amounts. Selenium protects intracellular structures against oxidative damage. It is an essential component of GLUTATHIONE PEROXIDASE.
An enzyme derived from cow's milk. It catalyzes the radioiodination of tyrosine and its derivatives and of peptides containing tyrosine.
A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID PEROXIDES and peroxinitrite. They are found in a wide range of organisms, such as BACTERIA; PLANTS; and MAMMALS. The enzyme requires the presence of a thiol-containing intermediate such as THIOREDOXIN as a reducing cofactor.
The most abundant natural aromatic organic polymer found in all vascular plants. Lignin together with cellulose and hemicellulose are the major cell wall components of the fibers of all wood and grass species. Lignin is composed of coniferyl, p-coumaryl, and sinapyl alcohols in varying ratios in different plant species. (From Merck Index, 11th ed)
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC 1.15.1.1.
An enzyme that catalyzes the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. EC 1.11.1.10.
A phylum of fungi that produce their sexual spores (basidiospores) on the outside of the basidium. It includes forms commonly known as mushrooms, boletes, puffballs, earthstars, stinkhorns, bird's-nest fungi, jelly fungi, bracket or shelf fungi, and rust and smut fungi.
Alcohols derived from the aryl radical (C6H5CH2-) and defined by C6H5CHOH. The concept includes derivatives with any substituents on the benzene ring.
Naturally occurring or synthetic substances that inhibit or retard the oxidation of a substance to which it is added. They counteract the harmful and damaging effects of oxidation in animal tissues.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
A group of compounds that contain a bivalent O-O group, i.e., the oxygen atoms are univalent. They can either be inorganic or organic in nature. Such compounds release atomic (nascent) oxygen readily. Thus they are strong oxidizing agents and fire hazards when in contact with combustible materials, especially under high-temperature conditions. The chief industrial uses of peroxides are as oxidizing agents, bleaching agents, and initiators of polymerization. (From Hawley's Condensed Chemical Dictionary, 11th ed)
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.
Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
The rate dynamics in chemical or physical systems.
A genus of fungi in the family Corticiaceae, order Stereales, that degrades lignin. The white-rot fungus Phanerochaete chrysosporium is a frequently used species in research.
Very toxic industrial chemicals. They are absorbed through the skin, causing lethal blood, bladder, liver, and kidney damage and are potent, broad-spectrum carcinogens in most species.
A genus of black-spored basidiomycetous fungi of the family Coprinaceae, order Agaricales; some species are edible.
Inorganic binary compounds of iodine or the I- ion.
Selenoproteins are proteins that specifically incorporate SELENOCYSTEINE into their amino acid chain. Most selenoproteins are enzymes with the selenocysteine residues being responsible for their catalytic functions.
Peroxides produced in the presence of a free radical by the oxidation of unsaturated fatty acids in the cell in the presence of molecular oxygen. The formation of lipid peroxides results in the destruction of the original lipid leading to the loss of integrity of the membranes. They therefore cause a variety of toxic effects in vivo and their formation is considered a pathological process in biological systems. Their formation can be inhibited by antioxidants, such as vitamin E, structural separation or low oxygen tension.
The lectin wheatgerm agglutinin conjugated to the enzyme HORSERADISH PEROXIDASE. It is widely used for tracing neural pathways.
A genus of basidiomycetous fungi, family POLYPORACEAE, order POLYPORALES, that grows on logs or tree stumps in shelflike layers. The species P. ostreatus, the oyster mushroom, is a choice edible species and is the most frequently encountered member of the genus in eastern North America. (Alexopoulos et al., Introductory Mycology, 4th ed, p531)
A selenium compound with the molecular formula H2SO3. It used as a source of SELENIUM, especially for patients that develop selenium deficiency following prolonged PARENTERAL NUTRITION.
Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated.
The dialdehyde of malonic acid.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A peroxiredoxin that is a cytosolic bifunctional enzyme. It functions as a peroxiredoxin via a single redox-active cysteine and also contains a Ca2+-independent acidic phospholipase A2 activity.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A highly vascularized endocrine gland consisting of two lobes joined by a thin band of tissue with one lobe on each side of the TRACHEA. It secretes THYROID HORMONES from the follicular cells and CALCITONIN from the parafollicular cells thereby regulating METABOLISM and CALCIUM level in blood, respectively.
'3,3'-Diaminobenzidine (DAB) is a chemical compound used in histology and immunohistochemistry as a chromogen for the visualization of an antigen-antibody reaction, where it forms an insoluble brown precipitate at the site of the reaction, facilitating microscopic analysis.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
A THIOREDOXIN-dependent hydroperoxidase that is localized in the mitochondrial matrix. The enzyme plays a crucial role in protecting mitochondrial components from elevated levels of HYDROGEN PEROXIDE.
An extracellular selenoprotein that contains most of the SELENIUM in PLASMA. Selenoprotein P functions as an antioxidant and appears to transport selenium from the LIVER to peripheral tissues.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
A naturally occurring amino acid in both eukaryotic and prokaryotic organisms. It is found in tRNAs and in the catalytic site of some enzymes. The genes for glutathione peroxidase and formate dehydrogenase contain the TGA codon, which codes for this amino acid.
A family of bracket fungi, order POLYPORALES, living in decaying plant matter and timber.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant.
An order of fungi in the phylum BASIDIOMYCOTA having macroscopic basidiocarps. The members are characterized by their saprophytic activities as decomposers, particularly in the degradation of CELLULOSE and LIGNIN. A large number of species in the order have been used medicinally. (From Alexopoulos, Introductory Mycology, 4th ed, pp504-68)
Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.
Low-molecular-weight end products, probably malondialdehyde, that are formed during the decomposition of lipid peroxidation products. These compounds react with thiobarbituric acid to form a fluorescent red adduct.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
An enzyme of the oxidoreductase class that catalyzes the conversion of beta-D-glucose and oxygen to D-glucono-1,5-lactone and peroxide. It is a flavoprotein, highly specific for beta-D-glucose. The enzyme is produced by Penicillium notatum and other fungi and has antibacterial activity in the presence of glucose and oxygen. It is used to estimate glucose concentration in blood or urine samples through the formation of colored dyes by the hydrogen peroxide produced in the reaction. (From Enzyme Nomenclature, 1992) EC 1.1.3.4.
Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical.
Granular leukocytes with a nucleus that usually has two lobes connected by a slender thread of chromatin, and cytoplasm containing coarse, round granules that are uniform in size and stainable by eosin.
Enzymes which are immobilized on or in a variety of water-soluble or water-insoluble matrices with little or no loss of their catalytic activity. Since they can be reused continuously, immobilized enzymes have found wide application in the industrial, medical and research fields.
A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035)
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
An extensive order of basidiomycetous fungi whose fruiting bodies are commonly called mushrooms.
A direct-acting oxidative stress-inducing agent used to examine the effects of oxidant stress on Ca(2+)-dependent signal transduction in vascular endothelial cells. It is also used as a catalyst in polymerization reactions and to introduce peroxy groups into organic molecules.
A plant genus of the family BRASSICACEAE known for the root used in hot SPICES. It is also the source of HORSERADISH PEROXIDASE which is widely used in laboratories.
Thyroglobulin is a glycoprotein synthesized and secreted by thyroid follicular cells, serving as a precursor for the production of thyroid hormones T3 and T4, and its measurement in blood serves as a tumor marker for thyroid cancer surveillance.
Organic derivatives of thiocyanic acid which contain the general formula R-SCN.
Diagnostic aid in pancreas function determination.
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
Inorganic salts of the hypothetical acid ferrocyanic acid (H4Fe(CN)6).
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Electron-accepting molecules in chemical reactions in which electrons are transferred from one molecule to another (OXIDATION-REDUCTION).
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Benzene derivatives that include one or more hydroxyl groups attached to the ring structure.
A copper-containing oxidoreductase enzyme that catalyzes the oxidation of 4-benzenediol to 4-benzosemiquinone. It also has activity towards a variety of O-quinols and P-quinols. It primarily found in FUNGI and is involved in LIGNIN degradation, pigment biosynthesis and detoxification of lignin-derived products.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
The engulfing of liquids by cells by a process of invagination and closure of the cell membrane to form fluid-filled vacuoles.
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.
A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
A group of compounds that are derivatives of methoxybenzene and contain the general formula R-C7H7O.
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The disodium salt of selenious acid. It is used therapeutically to supply the trace element selenium and is prepared by the reaction of SELENIUM DIOXIDE with SODIUM HYDROXIDE.
A non-selective post-emergence, translocated herbicide. According to the Seventh Annual Report on Carcinogens (PB95-109781, 1994) this substance may reasonably be anticipated to be a carcinogen. (From Merck Index, 12th ed) It is an irreversible inhibitor of CATALASE, and thus impairs activity of peroxisomes.
Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.
'Benzene derivatives' are organic compounds that contain a benzene ring as the core structure, with various functional groups attached to it, and can have diverse chemical properties and uses, including as solvents, intermediates in chemical synthesis, and pharmaceuticals.
Inflammatory disease of the THYROID GLAND due to autoimmune responses leading to lymphocytic infiltration of the gland. It is characterized by the presence of circulating thyroid antigen-specific T-CELLS and thyroid AUTOANTIBODIES. The clinical signs can range from HYPOTHYROIDISM to THYROTOXICOSIS depending on the type of autoimmune thyroiditis.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.
Salts of hydrobromic acid, HBr, with the bromine atom in the 1- oxidation state. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A generic descriptor for all TOCOPHEROLS and TOCOTRIENOLS that exhibit ALPHA-TOCOPHEROL activity. By virtue of the phenolic hydrogen on the 2H-1-benzopyran-6-ol nucleus, these compounds exhibit varying degree of antioxidant activity, depending on the site and number of methyl groups and the type of ISOPRENOIDS.
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
A genus of fungi in the family Coriolaceae.
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Organic compounds which contain selenium as an integral part of the molecule.
Proteins prepared by recombinant DNA technology.
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5
A group of physiologically active prostaglandin endoperoxides. They are precursors in the biosynthesis of prostaglandins and thromboxanes. Most frequently encountered member of this group is the prostaglandin G2.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Compounds containing the -SH radical.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
Diazo derivatives of aniline, used as a reagent for sugars, ketones, and aldehydes. (Dorland, 28th ed)
A plant genus in the family LILIACEAE (sometimes placed in Asparagaceae) that contains ECDYSTEROIDS and is an ingredient of Siotone. The shoots are used as a vegetable and the roots are used in FOLK MEDICINE.
Elements of limited time intervals, contributing to particular results or situations.
Hydroxycinnamic acid and its derivatives. Act as activators of the indoleacetic acid oxidizing system, thereby producing a decrease in the endogenous level of bound indoleacetic acid in plants.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
An antiseptic and disinfectant aromatic alcohol.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
A cytochrome oxidase inhibitor which is a nitridizing agent and an inhibitor of terminal oxidation. (From Merck Index, 12th ed)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A product from the iodination of MONOIODOTYROSINE. In the biosynthesis of thyroid hormones, diiodotyrosine residues are coupled with other monoiodotyrosine or diiodotyrosine residues to form T4 or T3 thyroid hormones (THYROXINE and TRIIODOTHYRONINE).
The marking of biological material with a dye or other reagent for the purpose of identifying and quantitating components of tissues, cells or their extracts.

Human granulocytic ehrlichiosis agent and Ehrlichia chaffeensis reside in different cytoplasmic compartments in HL-60 cells. (1/3678)

The human granulocytic ehrlichiosis (HGE) agent resides and multiplies exclusively in cytoplasmic vacuoles of granulocytes. Double immunofluorescence labeling was used to characterize the nature of the HGE agent replicative inclusions and to compare them with inclusions containing the human monocytic ehrlichia, Ehrlichia chaffeensis, in HL-60 cells. Although both Ehrlichia spp. can coinfect HL-60 cells, they resided in separate inclusions. Inclusions of both Ehrlichia spp. were not labeled with either anti-lysosome-associated membrane protein 1 or anti-CD63. Accumulation of myeloperoxidase-positive granules were seen around HGE agent inclusions but not around E. chaffeensis inclusions. 3-(2, 4-Dinitroanilino)-3'-amino-N-methyldipropylamine and acridine orange were not localized to either inclusion type. Vacuolar-type H+-ATPase was not colocalized with HGE agent inclusions but was weakly colocalized with E. chaffeensis inclusions. E. chaffeensis inclusions were labeled with the transferrin receptor, early endosomal antigen 1, and rab5, but HGE agent inclusions were not. Some HGE agent and E. chaffeensis inclusions colocalized with major histocompatibility complex class I and II antigens. These two inclusions were not labeled for annexins I, II, IV, and VI; alpha-adaptin; clathrin heavy chain; or beta-coatomer protein. Vesicle-associated membrane protein 2 colocalized to both inclusions. The cation-independent mannose 6-phosphate receptor was not colocalized with either inclusion type. Endogenously synthesized sphingomyelin, from C6-NBD-ceramide, was not incorporated into either inclusion type. Brefeldin A did not affect the growth of either Ehrlichia sp. in HL-60 cells. These results suggest that the HGE agent resides in inclusions which are neither early nor late endosomes and does not fuse with lysosomes or Golgi-derived vesicles, while E. chaffeensis resides in an early endosomal compartment which accumulates the transferrin receptor.  (+info)

Alternating antineutrophil cytoplasmic antibody specificity: drug-induced vasculitis in a patient with Wegener's granulomatosis. (2/3678)

We describe a patient who presented with Wegener's granulomatosis associated with antineutrophil cytoplasmic antibodies (ANCA) directed against proteinase 3 (PR3) with a cytoplasmic immunofluorescence pattern (cANCA), whose ANCA type changed to antimyeloperoxidase antibodies with a perinuclear immunofluorescence pattern (pANCA) when treated with propylthiouracil, and changed back to anti-PR3 antibodies with cANCA after the medication was discontinued. The patient developed flares of vasculitis symptoms associated with rises in either type of ANCA. Tests for antimyeloperoxidase ANCA were repeatedly negative before the drug was started, strongly implicating the drug as the cause of the episode. This case demonstrates that patients with idiopathic ANCA-positive vasculitis may quickly develop a superimposed drug-associated ANCA-positive vasculitis. Iatrogenic vasculitis should be suspected when a patient with idiopathic vasculitis with one type of ANCA develops the other type of ANCA.  (+info)

Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II. (3/3678)

Myeloperoxidase (MPO) is the most abundant protein in neutrophils and plays a central role in microbial killing and inflammatory tissue damage. Because most of the non-steroidal anti-inflammatory drugs and other drugs contain a thiol group, it is necessary to understand how these substrates are oxidized by MPO. We have performed transient kinetic measurements to study the oxidation of 14 aliphatic and aromatic mono- and dithiols by the MPO intermediates, Compound I (k3) and Compound II (k4), using sequential mixing stopped-flow techniques. The one-electron reduction of Compound I by aromatic thiols (e.g. methimidazole, 2-mercaptopurine and 6-mercaptopurine) varied by less than a factor of seven (between 1.39 +/- 0.12 x 10(5) M(-1) s(-1) and 9.16 +/- 1.63 x 10(5) M(-1) s(-1)), whereas reduction by aliphatic thiols was demonstrated to depend on their overall net charge and hydrophobic character and not on the percentage of thiol deprotonation or redox potential. Cysteamine, cysteine methyl ester, cysteine ethyl ester and alpha-lipoic acid showed k3 values comparable to aromatic thiols, whereas a free carboxy group (e.g. cysteine, N-acetylcysteine, glutathione) diminished k3 dramatically. The one-electron reduction of Compound II was far more constrained by the nature of the substrate. Reduction by methimidazole, 2-mercaptopurine and 6-mercaptopurine showed second-order rate constants (k4) of 1.33 +/- 0.08 x 10(5) M(-1) s(-1), 5.25 +/- 0.07 x 10(5) M(-1) s(-1) and 3.03 +/- 0.07 x 10(3) M(-1) s(-1). Even at high concentrations cysteine, penicillamine and glutathione could not reduce Compound II, whereas cysteamine (4.27 +/- 0.05 x 10(3) M(-1) s(-1)), cysteine methyl ester (8.14 +/- 0.08 x 10(3) M(-1) s(-1)), cysteine ethyl ester (3.76 +/- 0.17 x 10(3) M(-1) s(-1)) and alpha-lipoic acid (4.78 +/- 0.07 x 10(4) M(-1) s(-1)) were demonstrated to reduce Compound II and thus could be expected to be oxidized by MPO without co-substrates.  (+info)

The inhibition of myeloperoxidase by ceruloplasmin can be reversed by anti-myeloperoxidase antibodies. (4/3678)

BACKGROUND: The purpose of this study was to characterize the recently reported inhibition of myeloperoxidase (MPO) by ceruloplasmin and to determine whether this may be disturbed in the presence of anti-MPO antibodies. METHODS: Specificity of the binding between ceruloplasmin and MPO was confirmed by Western blotting and enzyme-linked immunosorbent assay (ELISA), and the enzymatic activity of MPO was measured in the presence of ceruloplasmin, affinity-purified anti-MPO antibodies, or both. The affinity of the binding between MPO and ceruloplasmin and MPO and the anti-MPO antibodies was measured using a biosensor, with the results confirmed by chaotrope ELISA. RESULTS: Affinity-purified anti-MPO antibodies from patients with microscopic polyangiitis and florid renal vasculitis inhibited the binding between ceruloplasmin and MPO to a maximum of 72.9 +/- 12.8%, whereas those from patients with Wegener's granulomatosis and only minimal renal involvement inhibited the binding to a maximum of only 36.8 +/- 10.9% (P < 0. 001), with comparable reversal of the ceruloplasmin-mediated inhibition of MPO activity. Measurement of the affinity of the interactions demonstrated that binding between MPO and the anti-MPO antibodies is stronger than that between MPO and ceruloplasmin (1.61 x 107 to 1.33 x 108 vs. 7.46 x 106 m-1), indicating that binding to the autoantibody would be favored in vivo. CONCLUSIONS: This study confirms a role for ceruloplasmin as a physiological inhibitor of MPO, and demonstrates how the inhibition may be disrupted in the presence of anti-MPO antibodies. Because a majority (16 of 21) of the antibodies did not themselves inhibit MPO activity, their interference with the inhibition mediated by ceruloplasmin may be brought about by steric hindrance consequent upon the binding of the antibody to a dominant epitope at or near the active site.  (+info)

A cell-surface superoxide dismutase is a binding protein for peroxinectin, a cell-adhesive peroxidase in crayfish. (5/3678)

Peroxinectin, a cell-adhesive peroxidase (homologous to human myeloperoxidase), from the crayfish Pacifastacus leniusculus, was shown by immuno-fluorescence to bind to the surface of crayfish blood cells (haemocytes). In order to identify a cell surface receptor for peroxinectin, labelled peroxinectin was incubated with a blot of haemocyte membrane proteins. It was found to specifically bind two bands of 230 and 90 kDa; this binding was decreased in the presence of unlabelled peroxinectin. Purified 230/90 kDa complex also bound peroxinectin in the same assay. In addition, the 230 kDa band binds the crayfish beta-1,3-glucan-binding protein. The 230 kDa band could be reduced to 90 kDa, thus showing that the 230 kDa is a multimer of 90 kDa units. The peroxinectin-binding protein was cloned from a haemocyte cDNA library, using immuno-screening or polymerase chain reaction based on partial amino acid sequence of the purified protein. It has a signal sequence, a domain homologous to CuZn-containing superoxide dismutases, and a basic, proline-rich, C-terminal tail, but no membrane-spanning segment. In accordance, the 90 and 230 kDa bands had superoxide dismutase activity. Immuno-fluorescence of non-permeabilized haemocytes with affinity-purified antibodies confirmed that the crayfish CuZn-superoxide dismutase is localized at the cell surface; it could be released from the membrane with high salt. It was thus concluded that the peroxinectin-binding protein is an extracellular SOD (EC-SOD) and a peripheral membrane protein, presumably kept at the cell surface via ionic interaction with its C-terminal region. This interaction with a peroxidase seems to be a novel function for an SOD. The binding of the cell surface SOD to the cell-adhesive/opsonic peroxinectin may mediate, or regulate, cell adhesion and phagocytosis; it may also be important for efficient localized production of microbicidal substances.  (+info)

Cloning and characterization of a cDNA encoding a novel extracellular peroxidase from Trametes versicolor. (6/3678)

The white rot basidiomycete Trametes versicolor secretes a large number of peroxidases which are believed to be involved in the degradation of polymeric lignin. These peroxidases have been classified previously as lignin peroxidases or manganese peroxidases (MnP). We have isolated a novel extracellular peroxidase-encoding cDNA sequence from T. versicolor CU1, the transcript levels of which are repressed by low concentrations of Mn2+ and induced by nitrogen and carbon but not induced in response to a range of stresses which have been reported to induce MnP expression.  (+info)

Expression of the cell adhesion molecules on leukocytes that demarginate during acute maximal exercise. (7/3678)

The pulmonary vascular bed is an important reservoir for the marginated pool of leukocytes that can be mobilized by exercise or catecholamines. This study was designed to determine the phenotypic characteristics of leukocytes that are mobilized into the circulation during exercise. Twenty healthy volunteers performed incremental exercise to exhaustion [maximal O2 consumption (VO2 max)] on a cycle ergometer. Blood was collected at baseline, at 3-min intervals during exercise, at VO2 max, and 30 min after exercise. Total white cell, polymorphonuclear leukocyte (PMN), and lymphocyte counts increased with exercise to VO2 max (P < 0.05). Flow cytometric analysis showed that the mean fluorescence intensity of L-selectin on PMN (from 14.9 +/- 1 at baseline to 9.5 +/- 1.6 at VO2 max, P < 0.05) and lymphocytes (from 11.7 +/- 1.2 at baseline to 8 +/- 0.8 at VO2 max, P < 0.05) decreased with exercise. Mean fluorescence intensity of CD11b on PMN increased with exercise (from 10.2 +/- 0.6 at baseline to 25 +/- 2.5 at VO2 max, P < 0.002) but remained unchanged on lymphocytes. Myeloperoxidase levels in PMN did not change with exercise. In vitro studies showed that neither catecholamines nor plasma collected at VO2 max during exercise changed leukocyte L-selectin or CD11b levels. We conclude that PMN released from the marginated pool during exercise express low levels of L-selectin and high levels of CD11b.  (+info)

Purification and cloning of the salivary peroxidase/catechol oxidase of the mosquito Anopheles albimanus. (8/3678)

Salivary homogenates of the adult female mosquito Anopheles albimanus have been shown previously to contain a vasodilatory activity associated with a catechol oxidase/peroxidase activity. We have now purified the salivary peroxidase using high-performance liquid chromatography. The pure enzyme is able to relax rabbit aortic rings pre-constricted with norepinephrine. The peroxidase has a relative molecular mass of 66 907 as estimated by mass spectrometry. Amino-terminal sequencing allowed us to design oligonucleotide probes for isolation of cDNA clones derived from the salivary gland mRNA from female mosquitoes. The full sequence of the cDNA demonstrated homology between A. albimanus salivary peroxidase and several members of the myeloperoxidase gene family. A close comparison of A. albimanus salivary peroxidase with canine myeloperoxidase, for which the crystal structure is known, showed that all six disulfide bridges were conserved and demonstrated identity for all five residues associated with a Ca2+-binding site. In addition, 16 of 26 residues shown to be in close proximity to the heme moiety in the canine myeloperoxidase were identical. We conclude that the salivary peroxidase of A. albimanus belongs to the myeloperoxidase gene family. Other possible functions for this molecule in blood feeding are discussed.  (+info)

Peroxidases are a group of enzymes that catalyze the oxidation of various substrates using hydrogen peroxide (H2O2) as the electron acceptor. These enzymes contain a heme prosthetic group, which plays a crucial role in their catalytic activity. Peroxidases are widely distributed in nature and can be found in plants, animals, and microorganisms. They play important roles in various biological processes, including defense against oxidative stress, lignin degradation, and host-pathogen interactions. Some common examples of peroxidases include glutathione peroxidase, which helps protect cells from oxidative damage, and horseradish peroxidase, which is often used in laboratory research.

Horseradish peroxidase (HRP) is not a medical term, but a type of enzyme that is derived from the horseradish plant. In biological terms, HRP is defined as a heme-containing enzyme isolated from the roots of the horseradish plant (Armoracia rusticana). It is widely used in molecular biology and diagnostic applications due to its ability to catalyze various oxidative reactions, particularly in immunological techniques such as Western blotting and ELISA.

HRP catalyzes the conversion of hydrogen peroxide into water and oxygen, while simultaneously converting a variety of substrates into colored or fluorescent products that can be easily detected. This enzymatic activity makes HRP a valuable tool in detecting and quantifying specific biomolecules, such as proteins and nucleic acids, in biological samples.

Glutathione peroxidase (GPx) is a family of enzymes with peroxidase activity whose main function is to protect the organism from oxidative damage. They catalyze the reduction of hydrogen peroxide, lipid peroxides, and organic hydroperoxides to water or corresponding alcohols, using glutathione (GSH) as a reducing agent, which is converted to its oxidized form (GSSG). There are several isoforms of GPx found in different tissues, including GPx1 (also known as cellular GPx), GPx2 (gastrointestinal GPx), GPx3 (plasma GPx), GPx4 (also known as phospholipid hydroperoxide GPx), and GPx5-GPx8. These enzymes play crucial roles in various biological processes, such as antioxidant defense, cell signaling, and apoptosis regulation.

Peroxidase is a type of enzyme that catalyzes the chemical reaction in which hydrogen peroxide (H2O2) is broken down into water (H2O) and oxygen (O2). This enzymatic reaction also involves the oxidation of various organic and inorganic compounds, which can serve as electron donors.

Peroxidases are widely distributed in nature and can be found in various organisms, including bacteria, fungi, plants, and animals. They play important roles in various biological processes, such as defense against oxidative stress, breakdown of toxic substances, and participation in metabolic pathways.

The peroxidase-catalyzed reaction can be represented by the following chemical equation:

H2O2 + 2e- + 2H+ → 2H2O

In this reaction, hydrogen peroxide is reduced to water, and the electron donor is oxidized. The peroxidase enzyme facilitates the transfer of electrons between the substrate (hydrogen peroxide) and the electron donor, making the reaction more efficient and specific.

Peroxidases have various applications in medicine, industry, and research. For example, they can be used for diagnostic purposes, as biosensors, and in the treatment of wastewater and medical wastes. Additionally, peroxidases are involved in several pathological conditions, such as inflammation, cancer, and neurodegenerative diseases, making them potential targets for therapeutic interventions.

Cytochrome-c peroxidase is an enzyme found in the inner membrane of mitochondria, which are the energy-producing structures in cells. It plays a crucial role in the electron transport chain, a series of complexes that generate energy in the form of ATP through a process called oxidative phosphorylation.

The enzyme's primary function is to catalyze the conversion of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect the cell from the harmful effects of hydrogen peroxide, which can damage proteins, lipids, and DNA if left unchecked.

Cytochrome-c peroxidase contains a heme group, which is a prosthetic group consisting of an iron atom surrounded by a porphyrin ring. This heme group is responsible for the enzyme's ability to undergo redox reactions, where it cycles between its oxidized and reduced states during the catalytic cycle.

The medical relevance of cytochrome-c peroxidase lies in its role in cellular metabolism and energy production. Dysfunctions in the electron transport chain or oxidative phosphorylation processes, including those involving cytochrome-c peroxidase, can lead to various mitochondrial disorders and diseases, such as neurodegenerative conditions, muscle weakness, and metabolic abnormalities. However, it is essential to note that the study of this enzyme and its role in health and disease is still an active area of research.

Ascorbate peroxidases (AHPX) are a group of enzymes that use ascorbic acid (vitamin C) as a reducing cofactor to catalyze the conversion of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from oxidative damage caused by the accumulation of H2O2, a byproduct of various metabolic processes. Ascorbate peroxidases are primarily found in plants, algae, and cyanobacteria, where they play a crucial role in the detoxification of reactive oxygen species generated during photosynthesis.

Eosinophil peroxidase (EPO) is an enzyme that is primarily found in the granules of eosinophils, which are a type of white blood cell that plays a role in the immune response. EPO is involved in the destruction of certain types of parasites and also contributes to the inflammatory response in allergic reactions and other diseases.

EPO catalyzes the conversion of hydrogen peroxide to hypochlorous acid, which is a potent oxidizing agent that can kill or inhibit the growth of microorganisms. EPO also plays a role in the production of other reactive oxygen species, which can contribute to tissue damage and inflammation in certain conditions.

Elevated levels of EPO in tissues or bodily fluids may be indicative of eosinophil activation and degranulation, which can occur in various diseases such as asthma, allergies, parasitic infections, and some types of cancer. Measuring EPO levels can be useful in the diagnosis and monitoring of these conditions.

Iodide peroxidase, also known as iodide:hydrogen peroxide oxidoreductase, is an enzyme that belongs to the family of oxidoreductases. Specifically, it is a peroxidase that uses iodide as its physiological reducing substrate. This enzyme catalyzes the oxidation of iodide by hydrogen peroxide to produce iodine, which plays a crucial role in thyroid hormone biosynthesis.

The systematic name for this enzyme is iodide:hydrogen-peroxide oxidoreductase (iodinating). It is most commonly found in the thyroid gland, where it helps to produce and regulate thyroid hormones by facilitating the iodination of tyrosine residues on thyroglobulin, a protein produced by the thyroid gland.

Iodide peroxidase requires a heme cofactor for its enzymatic activity, which is responsible for the oxidation-reduction reactions it catalyzes. The enzyme's ability to iodinate tyrosine residues on thyroglobulin is essential for the production of triiodothyronine (T3) and thyroxine (T4), two critical hormones that regulate metabolism, growth, and development in mammals.

Hydrogen peroxide (H2O2) is a colorless, odorless, clear liquid with a slightly sweet taste, although drinking it is harmful and can cause poisoning. It is a weak oxidizing agent and is used as an antiseptic and a bleaching agent. In diluted form, it is used to disinfect wounds and kill bacteria and viruses on the skin; in higher concentrations, it can be used to bleach hair or remove stains from clothing. It is also used as a propellant in rocketry and in certain industrial processes. Chemically, hydrogen peroxide is composed of two hydrogen atoms and two oxygen atoms, and it is structurally similar to water (H2O), with an extra oxygen atom. This gives it its oxidizing properties, as the additional oxygen can be released and used to react with other substances.

Guaiacol is not a medical term per se, but it is a chemical compound with potential applications in the medical field. Here's a general definition:

Guaiacol (also known as 2-methoxyphenol) is an organic compound that belongs to the class of phenols. It is a colorless or slightly yellow oily liquid with a characteristic smoky odor, and it is soluble in alcohol and ether but only sparingly soluble in water. Guaiacol occurs naturally in the smoke of wood fires and is also found in certain plants, such as guaiacum and creosote bush. It has antimicrobial properties and is used in some medical and industrial applications, including as a precursor for the synthesis of other chemicals.

Catalase is a type of enzyme that is found in many living organisms, including humans. Its primary function is to catalyze the decomposition of hydrogen peroxide (H2O2) into water (H2O) and oxygen (O2). This reaction helps protect cells from the harmful effects of hydrogen peroxide, which can be toxic at high concentrations.

The chemical reaction catalyzed by catalase can be represented as follows:

H2O2 + Catalase → H2O + O2 + Catalase

Catalase is a powerful antioxidant enzyme that plays an important role in protecting cells from oxidative damage. It is found in high concentrations in tissues that produce or are exposed to hydrogen peroxide, such as the liver, kidneys, and erythrocytes (red blood cells).

Deficiency in catalase activity has been linked to several diseases, including cancer, neurodegenerative disorders, and aging. On the other hand, overexpression of catalase has been shown to have potential therapeutic benefits in various disease models, such as reducing inflammation and oxidative stress.

Selenium is a trace element that is essential for the proper functioning of the human body. According to the medical definitions provided by the National Institutes of Health (NIH), selenium is a component of several major metabolic pathways, including thyroid hormone metabolism, antioxidant defense systems, and immune function.

Selenium is found in a variety of foods, including nuts (particularly Brazil nuts), cereals, fish, and meat. It exists in several forms, with selenomethionine being the most common form found in food. Other forms include selenocysteine, which is incorporated into proteins, and selenite and selenate, which are inorganic forms of selenium.

The recommended dietary allowance (RDA) for selenium is 55 micrograms per day for adults. While selenium deficiency is rare, chronic selenium deficiency can lead to conditions such as Keshan disease, a type of cardiomyopathy, and Kaschin-Beck disease, which affects the bones and joints.

It's important to note that while selenium is essential for health, excessive intake can be harmful. High levels of selenium can cause symptoms such as nausea, vomiting, hair loss, and neurological damage. The tolerable upper intake level (UL) for selenium is 400 micrograms per day for adults.

Lactoperoxidase is a type of peroxidase enzyme that is present in various secretory fluids, including milk, saliva, and tears. In milk, lactoperoxidase plays an important role in the natural defense system by helping to protect against microbial growth. It does this by catalyzing the oxidation of thiocyanate ions (SCN-) in the presence of hydrogen peroxide (H2O2) to produce hypothiocyanite (OSCN-), which is a potent antimicrobial agent.

Lactoperoxidase is a glycoprotein with a molecular weight of approximately 78 kDa, and it is composed of four identical subunits, each containing a heme group that binds to the hydrogen peroxide molecule during the enzymatic reaction. Lactoperoxidase has been studied for its potential therapeutic applications in various fields, including oral health, food preservation, and wound healing.

Peroxiredoxins (Prx) are a family of peroxidases that play a crucial role in cellular defense against oxidative stress. They catalyze the reduction of hydrogen peroxide, organic hydroperoxides, and peroxynitrite, thereby protecting cells from potentially harmful effects of these reactive oxygen and nitrogen species.

Peroxiredoxins are ubiquitously expressed in various cellular compartments, including the cytosol, mitochondria, and nucleus. They contain a conserved catalytic cysteine residue that gets oxidized during the reduction of peroxides, which is then reduced back to its active form by thioredoxins or other reducing agents.

Dysregulation of peroxiredoxin function has been implicated in various pathological conditions, including cancer, neurodegenerative diseases, and inflammatory disorders. Therefore, understanding the role of peroxiredoxins in cellular redox homeostasis is essential for developing novel therapeutic strategies to treat oxidative stress-related diseases.

I'm sorry for any confusion, but "Lignin" is not a medical term. It is a term used in the field of biology and chemistry, particularly in botany and wood science. Lignin is a complex organic polymer that binds cellulose fibers together, providing strength and rigidity to the cell walls of plants. It is a major component of wood and bark.

If you have any medical terms you would like defined or any other questions, please let me know!

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Medical Definition:

Superoxide dismutase (SOD) is an enzyme that catalyzes the dismutation of superoxide radicals (O2-) into oxygen (O2) and hydrogen peroxide (H2O2). This essential antioxidant defense mechanism helps protect the body's cells from damage caused by reactive oxygen species (ROS), which are produced during normal metabolic processes and can lead to oxidative stress when their levels become too high.

There are three main types of superoxide dismutase found in different cellular locations:
1. Copper-zinc superoxide dismutase (CuZnSOD or SOD1) - Present mainly in the cytoplasm of cells.
2. Manganese superoxide dismutase (MnSOD or SOD2) - Located within the mitochondrial matrix.
3. Extracellular superoxide dismutase (EcSOD or SOD3) - Found in the extracellular spaces, such as blood vessels and connective tissues.

Imbalances in SOD levels or activity have been linked to various pathological conditions, including neurodegenerative diseases, cancer, and aging-related disorders.

Chloride peroxidase is an enzyme that contains heme as a cofactor and is responsible for catalyzing the oxidation of chloride ions (Cl-) to hypochlorous acid (HOCl) using hydrogen peroxide (H2O2) as a substrate. This reaction plays a crucial role in the microbial defense system of certain organisms, such as the halophilic archaea. The enzyme is also known as chloroperoxidase or CPO.

The chemical reaction catalyzed by chloride peroxidase can be represented as follows:

Cl- + H2O2 → HOCl + H2O

Hypochlorous acid is a powerful oxidizing agent that can kill or inhibit the growth of various microorganisms, making it an important component of the immune system in some organisms. Chloride peroxidase has attracted significant interest from researchers due to its potential applications in biotechnology and environmental protection, such as in the development of new disinfection methods and the removal of pollutants from water.

Basidiomycota is a phylum in the kingdom Fungi that consists of organisms commonly known as club fungi or club mushrooms. The name Basidiomycota is derived from the presence of a characteristic reproductive structure called a basidium, which is where spores are produced.

The basidiomycetes include many familiar forms such as mushrooms, toadstools, bracket fungi, and other types of polypores. They have a complex life cycle that involves both sexual and asexual reproduction. The sexual reproductive stage produces a characteristic fruiting body, which may be microscopic or highly visible, depending on the species.

Basidiomycota fungi play important ecological roles in decomposing organic matter, forming mutualistic relationships with plants, and acting as parasites on other organisms. Some species are economically important, such as edible mushrooms, while others can be harmful or even deadly to humans and animals.

Benzyl alcohol is an aromatic alcohol with the chemical formula C6H5CH2OH. It is a colorless liquid with a mild, pleasant odor and is used as a solvent and preservative in cosmetics, medications, and other products. Benzyl alcohol can also be found as a natural component of some essential oils, fruits, and teas.

Benzyl alcohol is not typically considered a "drug" or a medication, but it may have various pharmacological effects when used in certain medical contexts. For example, it has antimicrobial properties and is sometimes used as a preservative in injectable medications to prevent the growth of bacteria and fungi. It can also be used as a local anesthetic or analgesic in some topical creams and ointments.

It's important to note that benzyl alcohol can be harmful or fatal to infants and young children, especially when it is used in high concentrations or when it is introduced into the body through intravenous (IV) routes. Therefore, it should be used with caution in these populations and only under the guidance of a healthcare professional.

Antioxidants are substances that can prevent or slow damage to cells caused by free radicals, which are unstable molecules that the body produces as a reaction to environmental and other pressures. Antioxidants are able to neutralize free radicals by donating an electron to them, thus stabilizing them and preventing them from causing further damage to the cells.

Antioxidants can be found in a variety of foods, including fruits, vegetables, nuts, and grains. Some common antioxidants include vitamins C and E, beta-carotene, and selenium. Antioxidants are also available as dietary supplements.

In addition to their role in protecting cells from damage, antioxidants have been studied for their potential to prevent or treat a number of health conditions, including cancer, heart disease, and age-related macular degeneration. However, more research is needed to fully understand the potential benefits and risks of using antioxidant supplements.

Glutathione reductase (GR) is an enzyme that plays a crucial role in maintaining the cellular redox state. The primary function of GR is to reduce oxidized glutathione (GSSG) to its reduced form (GSH), which is an essential intracellular antioxidant. This enzyme utilizes nicotinamide adenine dinucleotide phosphate (NADPH) as a reducing agent in the reaction, converting it to NADP+. The medical definition of Glutathione Reductase is:

Glutathione reductase (GSR; EC 1.8.1.7) is a homodimeric flavoprotein that catalyzes the reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH) in the presence of NADPH as a cofactor. This enzyme is essential for maintaining the cellular redox balance and protecting cells from oxidative stress by regenerating the active form of glutathione, a vital antioxidant and detoxifying agent.

Oxidative stress is defined as an imbalance between the production of reactive oxygen species (free radicals) and the body's ability to detoxify them or repair the damage they cause. This imbalance can lead to cellular damage, oxidation of proteins, lipids, and DNA, disruption of cellular functions, and activation of inflammatory responses. Prolonged or excessive oxidative stress has been linked to various health conditions, including cancer, cardiovascular diseases, neurodegenerative disorders, and aging-related diseases.

Heme is not a medical term per se, but it is a term used in the field of medicine and biology. Heme is a prosthetic group found in hemoproteins, which are proteins that contain a heme iron complex. This complex plays a crucial role in various biological processes, including oxygen transport (in hemoglobin), electron transfer (in cytochromes), and chemical catalysis (in peroxidases and catalases).

The heme group consists of an organic component called a porphyrin ring, which binds to a central iron atom. The iron atom can bind or release electrons, making it essential for redox reactions in the body. Heme is also vital for the formation of hemoglobin and myoglobin, proteins responsible for oxygen transport and storage in the blood and muscles, respectively.

In summary, heme is a complex organic-inorganic structure that plays a critical role in several biological processes, particularly in electron transfer and oxygen transport.

Peroxides, in a medical context, most commonly refer to chemical compounds that contain the peroxide ion (O2−2). Peroxides are characterized by the presence of an oxygen-oxygen single bond and can be found in various substances.

In dentistry, hydrogen peroxide (H2O2) is a widely used agent for teeth whitening or bleaching due to its oxidizing properties. It can help remove stains and discoloration on the tooth surface by breaking down into water and oxygen-free radicals, which react with the stain molecules, ultimately leading to their oxidation and elimination.

However, it is essential to note that high concentrations of hydrogen peroxide or prolonged exposure can cause tooth sensitivity, irritation to the oral soft tissues, and potential damage to the dental pulp. Therefore, professional supervision and appropriate concentration control are crucial when using peroxides for dental treatments.

Glutathione is a tripeptide composed of three amino acids: cysteine, glutamic acid, and glycine. It is a vital antioxidant that plays an essential role in maintaining cellular health and function. Glutathione helps protect cells from oxidative stress by neutralizing free radicals, which are unstable molecules that can damage cells and contribute to aging and diseases such as cancer, heart disease, and dementia. It also supports the immune system, detoxifies harmful substances, and regulates various cellular processes, including DNA synthesis and repair.

Glutathione is found in every cell of the body, with particularly high concentrations in the liver, lungs, and eyes. The body can produce its own glutathione, but levels may decline with age, illness, or exposure to toxins. As such, maintaining optimal glutathione levels through diet, supplementation, or other means is essential for overall health and well-being.

Histochemistry is the branch of pathology that deals with the microscopic localization of cellular or tissue components using specific chemical reactions. It involves the application of chemical techniques to identify and locate specific biomolecules within tissues, cells, and subcellular structures. This is achieved through the use of various staining methods that react with specific antigens or enzymes in the sample, allowing for their visualization under a microscope. Histochemistry is widely used in diagnostic pathology to identify different types of tissues, cells, and structures, as well as in research to study cellular and molecular processes in health and disease.

Lipid peroxidation is a process in which free radicals, such as reactive oxygen species (ROS), steal electrons from lipids containing carbon-carbon double bonds, particularly polyunsaturated fatty acids (PUFAs). This results in the formation of lipid hydroperoxides, which can decompose to form a variety of compounds including reactive carbonyl compounds, aldehydes, and ketones.

Malondialdehyde (MDA) is one such compound that is commonly used as a marker for lipid peroxidation. Lipid peroxidation can cause damage to cell membranes, leading to changes in their fluidity and permeability, and can also result in the modification of proteins and DNA, contributing to cellular dysfunction and ultimately cell death. It is associated with various pathological conditions such as atherosclerosis, neurodegenerative diseases, and cancer.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

"Phanerochaete" is a genus of saprotrophic fungi in the family Phanerochaetaceae. These fungi are characterized by their ability to degrade lignocellulosic materials, making them important decomposers in many ecosystems. They produce various extracellular enzymes that break down complex polymers such as cellulose and lignin, which are abundant in plant biomass. The genus Phanerochaete includes several species with medical relevance due to their potential role in human health and disease. For instance, some species have been studied for their ability to produce bioactive compounds with antimicrobial or anti-inflammatory properties. However, it is important to note that most Phanerochaete species are not typically associated with human diseases and are generally considered to be beneficial organisms in natural environments.

Benzidines are a class of chemical compounds with the basic structure of two benzene rings linked by a central nitrogen atom. The term "benzidine" can refer specifically to the parent compound, but it is more commonly used as a general term for a group of related compounds known as benzidine congeners or benzidine derivatives.

Benzidines are primarily used in the manufacture of dyes and pigments, although they have also been used in some industrial and laboratory applications. Exposure to benzidines has been linked to an increased risk of bladder cancer and other health problems, so their use is regulated in many countries.

It's worth noting that the medical definition of "benzidines" primarily focuses on their chemical structure and potential health effects, rather than their specific medical uses or applications.

"Coprinus" is a genus of fungi in the family Agaricaceae. It includes several species commonly known as "ink caps" or "shaggy manes." These mushrooms are characterized by their slimy, shaggy caps and the dark ink-like liquid that oozes from the gills when they mature. Some species of Coprinus are edible and considered delicacies, while others can cause adverse reactions if consumed with alcohol. It's important to note that proper identification is necessary before consuming any wild mushrooms.

Iodides are chemical compounds that contain iodine in the form of an iodide ion (I-). Iodide ions are negatively charged ions that consist of one iodine atom and an extra electron. Iodides are commonly found in dietary supplements and medications, and they are often used to treat or prevent iodine deficiency. They can also be used as expectorants to help thin and loosen mucus in the respiratory tract. Examples of iodides include potassium iodide (KI) and sodium iodide (NaI).

Selenoproteins are a specific group of proteins that contain the essential micronutrient selenium in the form of selenocysteine (Sec), which is a naturally occurring amino acid. Selenocysteine is encoded by the opal codon UGA, which typically serves as a stop codon in mRNA.

There are 25 known human selenoproteins, and they play crucial roles in various physiological processes, including antioxidant defense, DNA synthesis, thyroid hormone metabolism, and immune function. Some of the well-known selenoproteins include glutathione peroxidases (GPxs), thioredoxin reductases (TrxRs), and iodothyronine deiodinases (IDIs).

The presence of selenocysteine in these proteins makes them particularly efficient at catalyzing redox reactions, which involve the gain or loss of electrons. This property is essential for their functions as antioxidants and regulators of cellular signaling pathways.

Deficiencies in selenium can lead to impaired function of selenoproteins, potentially resulting in various health issues, such as increased oxidative stress, weakened immune response, and disrupted thyroid hormone metabolism.

Lipid peroxides are chemical compounds that form when lipids (fats or fat-like substances) oxidize. This process, known as lipid peroxidation, involves the reaction of lipids with oxygen in a way that leads to the formation of hydroperoxides and various aldehydes, such as malondialdehyde.

Lipid peroxidation is a naturally occurring process that can also be accelerated by factors such as exposure to radiation, certain chemicals, or enzymatic reactions. It plays a role in many biological processes, including cell signaling and regulation of gene expression, but it can also contribute to the development of various diseases when it becomes excessive.

Examples of lipid peroxides include phospholipid hydroperoxides, cholesteryl ester hydroperoxides, and triglyceride hydroperoxides. These compounds are often used as markers of oxidative stress in biological systems and have been implicated in the pathogenesis of atherosclerosis, cancer, neurodegenerative diseases, and other conditions associated with oxidative damage.

Wheat Germ Agglutinin (WGA) is a lectin protein found in wheat germ, which binds specifically to certain sugars on the surface of cells. Horseradish Peroxidase (HRP) is an enzyme derived from horseradish that catalyzes the conversion of certain substrates, producing a chemiluminescent or colorimetric signal.

A WGA-HRP conjugate refers to the formation of a covalent bond between WGA and HRP, creating an immunoconjugate. This complex is often used as a detection tool in various assays, such as ELISA (Enzyme-Linked Immunosorbent Assay) or Western blotting, where it can bind to specific carbohydrates on the target molecule and catalyze a colorimetric or chemiluminescent reaction, allowing for the visualization of the target.

"Pleurotus" is not a medical term, but a genus of fungi commonly known as oyster mushrooms. These mushrooms are often consumed for their nutritional and potential medicinal benefits. However, in a medical context, if someone is referring to "pleural," it relates to the pleura, which is the double-layered serous membrane that surrounds the lungs and lines the inside of the chest wall. Any medical condition or disease affecting this area may be described as "pleural."

Selenious acid, also known as selenic acid or hydrogen selenite, is not a substance that has a widely accepted medical definition. However, it is a chemical compound with the formula H2SeO3. It is a colorless, odorless liquid that is used in some industrial processes and is highly toxic if ingested or inhaled.

In the context of human health, selenium is an essential trace element that plays a critical role in various biological processes, including antioxidant defense systems, thyroid hormone metabolism, and immune function. Selenium can be found in various forms, including selenomethionine, selenocysteine, and selenite.

Selenious acid is not a form of selenium that is typically used or encountered in medical or nutritional contexts. However, it is possible that small amounts of selenious acid may be produced as an intermediate during the metabolism of certain selenium compounds in the body.

Free radicals are molecules or atoms that have one or more unpaired electrons in their outermost shell, making them highly reactive. They can be formed naturally in the body through processes such as metabolism and exercise, or they can come from external sources like pollution, radiation, and certain chemicals. Free radicals can cause damage to cells and contribute to the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. Antioxidants are substances that can neutralize free radicals and help protect against their harmful effects.

Malondialdehyde (MDA) is a naturally occurring organic compound that is formed as a byproduct of lipid peroxidation, a process in which free radicals or reactive oxygen species react with polyunsaturated fatty acids. MDA is a highly reactive aldehyde that can modify proteins, DNA, and other biomolecules, leading to cellular damage and dysfunction. It is often used as a marker of oxidative stress in biological systems and has been implicated in the development of various diseases, including cancer, cardiovascular disease, and neurodegenerative disorders.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Peroxiredoxin VI (Prdx6) is an antioxidant enzyme that belongs to the peroxiredoxin family. It plays a crucial role in reducing and regulating the levels of hydrogen peroxide, lipid peroxides, and other reactive oxygen species (ROS) within cells. Prdx6 has both peroxidase and phospholipase A2 activities, which makes it unique among the peroxiredoxins. It is widely expressed in various tissues, including the lungs, liver, kidneys, and brain. In addition to its antioxidant function, Prdx6 also contributes to cellular signaling pathways, inflammation regulation, and membrane repair processes. Dysregulation of Prdx6 has been implicated in several diseases, such as cancer, neurodegenerative disorders, and lung injury.

Catalysis is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst, which remains unchanged at the end of the reaction. A catalyst lowers the activation energy required for the reaction to occur, thereby allowing the reaction to proceed more quickly and efficiently. This can be particularly important in biological systems, where enzymes act as catalysts to speed up metabolic reactions that are essential for life.

The thyroid gland is a major endocrine gland located in the neck, anterior to the trachea and extends from the lower third of the Adams apple to the suprasternal notch. It has two lateral lobes, connected by an isthmus, and sometimes a pyramidal lobe. This gland plays a crucial role in the metabolism, growth, and development of the human body through the production of thyroid hormones (triiodothyronine/T3 and thyroxine/T4) and calcitonin. The thyroid hormones regulate body temperature, heart rate, and the production of protein, while calcitonin helps in controlling calcium levels in the blood. The function of the thyroid gland is controlled by the hypothalamus and pituitary gland through the thyroid-stimulating hormone (TSH).

3,3'-Diaminobenzidine (DAB) is a chemical compound that is commonly used as a chromogen in histological and immunohistochemical staining techniques. It is a type of polymerization substrate that reacts with horseradish peroxidase (HRP) to produce an insoluble, dark-brown precipitate at the site of the antigen-antibody reaction. This allows for the visualization and localization of specific proteins or other antigens within tissue sections.

The chemical formula for DAB is C12H12N2O2, and it is a light-sensitive compound that should be handled and stored in a dark environment to prevent unwanted photochemical reactions. It is important to note that DAB is considered a potential carcinogen and should be handled with appropriate safety precautions, including the use of gloves, lab coats, and eye protection.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Electron Spin Resonance (ESR) Spectroscopy, also known as Electron Paramagnetic Resonance (EPR) Spectroscopy, is a technique used to investigate materials with unpaired electrons. It is based on the principle of absorption of energy by the unpaired electrons when they are exposed to an external magnetic field and microwave radiation.

In this technique, a sample is placed in a magnetic field and microwave radiation is applied. The unpaired electrons in the sample absorb energy and change their spin state when the energy of the microwaves matches the energy difference between the spin states. This absorption of energy is recorded as a function of the magnetic field strength, producing an ESR spectrum.

ESR spectroscopy can provide information about the number, type, and behavior of unpaired electrons in a sample, as well as the local environment around the electron. It is widely used in physics, chemistry, and biology to study materials such as free radicals, transition metal ions, and defects in solids.

Peroxiredoxin III (PrxIII) is an antioxidant enzyme that belongs to the peroxiredoxin family. It plays a crucial role in maintaining the redox balance within cells by reducing hydrogen peroxide and other organic peroxides into water and alcohol, respectively. PrxIII is primarily located in the mitochondrial matrix, where it protects against oxidative damage to proteins, lipids, and DNA caused by reactive oxygen species (ROS). It functions as a homodimer and contains a conserved catalytic cysteine residue that gets oxidized during the reduction of peroxides. This oxidized form can be reduced back to its active state by thioredoxin or other reducing agents, allowing PrxIII to continue scavenging ROS. Mutations in the PRDX3 gene, which encodes Peroxiredoxin III, have been associated with various pathological conditions, including neurodegenerative diseases and cancer.

Selenoprotein P is a protein that contains several selenocysteine residues and is encoded by the SEPP1 gene in humans. It is primarily synthesized in the liver and secreted into the bloodstream, where it functions as a major antioxidant and a selenium transport protein. Selenoprotein P plays a crucial role in protecting cells against oxidative stress and has been implicated in various physiological processes, including neuroprotection, fertility, and immune function. Additionally, selenoprotein P has been suggested as a potential biomarker for selenium status and oxidative stress in the body.

Isoenzymes, also known as isoforms, are multiple forms of an enzyme that catalyze the same chemical reaction but differ in their amino acid sequence, structure, and/or kinetic properties. They are encoded by different genes or alternative splicing of the same gene. Isoenzymes can be found in various tissues and organs, and they play a crucial role in biological processes such as metabolism, detoxification, and cell signaling. Measurement of isoenzyme levels in body fluids (such as blood) can provide valuable diagnostic information for certain medical conditions, including tissue damage, inflammation, and various diseases.

Heme proteins are a type of protein that contain a heme group, which is a prosthetic group composed of an iron atom contained in the center of a large organic ring called a porphyrin. The heme group gives these proteins their characteristic red color. Hemeproteins have various important functions in biological systems, including oxygen transport (e.g., hemoglobin), electron transfer (e.g., cytochromes), and enzymatic catalysis (e.g., peroxidases and catalases). The heme group can bind and release gases, such as oxygen and carbon monoxide, and can participate in redox reactions due to the ease with which iron can change its oxidation state.

Selenocysteine (Sec) is a rare, naturally occurring amino acid that contains selenium. It is encoded by the opal (TGA) codon, which typically signals stop translation in mRNA. However, when followed by a specific hairpin-like structure called the Sec insertion sequence (SECIS) element in the 3' untranslated region of the mRNA, the TGA codon is interpreted as a signal for selenocysteine incorporation during protein synthesis.

Selenocysteine plays an essential role in several enzymes involved in antioxidant defense and redox homeostasis, such as glutathione peroxidases, thioredoxin reductases, and iodothyronine deiodinases. These enzymes require selenocysteine for their catalytic activity due to its unique chemical properties, which allow them to neutralize harmful reactive oxygen species (ROS) and maintain proper cellular function.

In summary, selenocysteine is a specialized amino acid containing selenium that is encoded by the TGA codon in mRNA when accompanied by a SECIS element. It is crucial for the activity of several enzymes involved in antioxidant defense and redox homeostasis.

I apologize for any confusion, but "Polyporaceae" is not a medical term. It is a taxonomic category in mycology, which is the branch of biology that deals with the study of fungi.

Polyporaceae is a family of fungi that includes various types of polypores, which are characterized by having pores on the underside of their fruiting bodies (the above-ground reproductive structures) instead of gills. These fungi are mostly saprotrophic, meaning they decompose dead or decaying organic matter to obtain nutrients. Some species can also be parasitic and cause diseases in living trees.

Examples of genera within Polyporaceae include Trametes, Ganoderma, Fomes, and Irpex, among others. If you have any questions related to medical terminology or concepts, please feel free to ask!

Electron microscopy (EM) is a type of microscopy that uses a beam of electrons to create an image of the sample being examined, resulting in much higher magnification and resolution than light microscopy. There are several types of electron microscopy, including transmission electron microscopy (TEM), scanning electron microscopy (SEM), and reflection electron microscopy (REM).

In TEM, a beam of electrons is transmitted through a thin slice of the sample, and the electrons that pass through the sample are focused to form an image. This technique can provide detailed information about the internal structure of cells, viruses, and other biological specimens, as well as the composition and structure of materials at the atomic level.

In SEM, a beam of electrons is scanned across the surface of the sample, and the electrons that are scattered back from the surface are detected to create an image. This technique can provide information about the topography and composition of surfaces, as well as the structure of materials at the microscopic level.

REM is a variation of SEM in which the beam of electrons is reflected off the surface of the sample, rather than scattered back from it. This technique can provide information about the surface chemistry and composition of materials.

Electron microscopy has a wide range of applications in biology, medicine, and materials science, including the study of cellular structure and function, disease diagnosis, and the development of new materials and technologies.

Ascorbic acid is the chemical name for Vitamin C. It is a water-soluble vitamin that is essential for human health. Ascorbic acid is required for the synthesis of collagen, a protein that plays a role in the structure of bones, tendons, ligaments, and blood vessels. It also functions as an antioxidant, helping to protect cells from damage caused by free radicals.

Ascorbic acid cannot be produced by the human body and must be obtained through diet or supplementation. Good food sources of vitamin C include citrus fruits, strawberries, bell peppers, broccoli, and spinach.

In the medical field, ascorbic acid is used to treat or prevent vitamin C deficiency and related conditions, such as scurvy. It may also be used in the treatment of various other health conditions, including common cold, cancer, and cardiovascular disease, although its effectiveness for these uses is still a matter of scientific debate.

Polyporales is an order of class Agaricomycetes, division Basidiomycota, in the kingdom Fungi. This order consists of various wood-decay fungi, characterized by their typically annual growth rings and pores on the underside of the cap. The fruiting bodies or conks of these fungi can be either resupinate (crust-like) or pileate (cap-like). Polyporales includes several economically important species that cause decay in trees and timber, as well as some medicinal mushrooms. Examples of genera within this order include Polyporus, Trametes, Fomes, and Ganoderma.

Reactive Oxygen Species (ROS) are highly reactive molecules containing oxygen, including peroxides, superoxide, hydroxyl radical, and singlet oxygen. They are naturally produced as byproducts of normal cellular metabolism in the mitochondria, and can also be generated by external sources such as ionizing radiation, tobacco smoke, and air pollutants. At low or moderate concentrations, ROS play important roles in cell signaling and homeostasis, but at high concentrations, they can cause significant damage to cell structures, including lipids, proteins, and DNA, leading to oxidative stress and potential cell death.

Thiobarbituric acid reactive substances (TBARS) is not a medical term per se, but rather a method used to measure lipid peroxidation in biological samples. Lipid peroxidation is a process by which free radicals steal electrons from lipids, leading to cellular damage and potential disease progression.

The TBARS assay measures the amount of malondialdehyde (MDA), a byproduct of lipid peroxidation, that reacts with thiobarbituric acid (TBA) to produce a pink-colored complex. The concentration of this complex is then measured and used as an indicator of lipid peroxidation in the sample.

While TBARS has been widely used as a measure of oxidative stress, it has limitations, including potential interference from other compounds that can react with TBA and produce similar-colored complexes. Therefore, more specific and sensitive methods for measuring lipid peroxidation have since been developed.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Glucose oxidase (GOD) is an enzyme that catalyzes the oxidation of D-glucose to D-glucono-1,5-lactone, while reducing oxygen to hydrogen peroxide in the process. This reaction is a part of the metabolic pathway in some organisms that convert glucose into energy. The systematic name for this enzyme is D-glucose:oxygen 1-oxidoreductase.

Glucose oxidase is commonly found in certain fungi, such as Aspergillus niger, and it has various applications in industry, medicine, and research. For instance, it's used in the production of glucose sensors for monitoring blood sugar levels, in the detection and quantification of glucose in food and beverages, and in the development of biosensors for environmental monitoring.

It's worth noting that while glucose oxidase has many applications, it should not be confused with glutathione peroxidase, another enzyme involved in the reduction of hydrogen peroxide to water.

Cyanides are a group of chemical compounds that contain the cyano group, -CN, which consists of a carbon atom triple-bonded to a nitrogen atom. They are highly toxic and can cause rapid death due to the inhibition of cellular respiration. Cyanide ions (CN-) bind to the ferric iron in cytochrome c oxidase, a crucial enzyme in the electron transport chain, preventing the flow of electrons and the production of ATP, leading to cellular asphyxiation.

Common sources of cyanides include industrial chemicals such as hydrogen cyanide (HCN) and potassium cyanide (KCN), as well as natural sources like certain fruits, nuts, and plants. Exposure to high levels of cyanides can occur through inhalation, ingestion, or skin absorption, leading to symptoms such as headache, dizziness, nausea, vomiting, rapid heartbeat, seizures, coma, and ultimately death. Treatment for cyanide poisoning typically involves the use of antidotes that bind to cyanide ions and convert them into less toxic forms, such as thiosulfate and rhodanese.

Eosinophils are a type of white blood cell that play an important role in the body's immune response. They are produced in the bone marrow and released into the bloodstream, where they can travel to different tissues and organs throughout the body. Eosinophils are characterized by their granules, which contain various proteins and enzymes that are toxic to parasites and can contribute to inflammation.

Eosinophils are typically associated with allergic reactions, asthma, and other inflammatory conditions. They can also be involved in the body's response to certain infections, particularly those caused by parasites such as worms. In some cases, elevated levels of eosinophils in the blood or tissues (a condition called eosinophilia) can indicate an underlying medical condition, such as a parasitic infection, autoimmune disorder, or cancer.

Eosinophils are named for their staining properties - they readily take up eosin dye, which is why they appear pink or red under the microscope. They make up only about 1-6% of circulating white blood cells in healthy individuals, but their numbers can increase significantly in response to certain triggers.

Immobilized enzymes refer to enzymes that have been restricted or fixed in a specific location and are unable to move freely. This is typically achieved through physical or chemical methods that attach the enzyme to a solid support or matrix. The immobilization of enzymes can provide several advantages, including increased stability, reusability, and ease of separation from the reaction mixture.

Immobilized enzymes are widely used in various industrial applications, such as biotransformations, biosensors, and diagnostic kits. They can also be used for the production of pharmaceuticals, food additives, and other fine chemicals. The immobilization techniques include adsorption, covalent binding, entrapment, and cross-linking.

Adsorption involves physically attaching the enzyme to a solid support through weak forces such as van der Waals interactions or hydrogen bonding. Covalent binding involves forming chemical bonds between the enzyme and the support matrix. Entrapment involves encapsulating the enzyme within a porous matrix, while cross-linking involves chemically linking multiple enzyme molecules together to form a stable structure.

Overall, immobilized enzymes offer several advantages over free enzymes, including improved stability, reusability, and ease of separation from the reaction mixture, making them valuable tools in various industrial applications.

Manganese is not a medical condition, but it's an essential trace element that is vital for human health. Here is the medical definition of Manganese:

Manganese (Mn) is a trace mineral that is present in tiny amounts in the body. It is found mainly in bones, the liver, kidneys, and pancreas. Manganese helps the body form connective tissue, bones, blood clotting factors, and sex hormones. It also plays a role in fat and carbohydrate metabolism, calcium absorption, and blood sugar regulation. Manganese is also necessary for normal brain and nerve function.

The recommended dietary allowance (RDA) for manganese is 2.3 mg per day for adult men and 1.8 mg per day for adult women. Good food sources of manganese include nuts, seeds, legumes, whole grains, green leafy vegetables, and tea.

In some cases, exposure to high levels of manganese can cause neurological symptoms similar to Parkinson's disease, a condition known as manganism. However, this is rare and usually occurs in people who are occupationally exposed to manganese dust or fumes, such as welders.

Glutathione transferases (GSTs) are a group of enzymes involved in the detoxification of xenobiotics and endogenous compounds. They facilitate the conjugation of these compounds with glutathione, a tripeptide consisting of cysteine, glutamic acid, and glycine, which results in more water-soluble products that can be easily excreted from the body.

GSTs play a crucial role in protecting cells against oxidative stress and chemical injury by neutralizing reactive electrophilic species and peroxides. They are found in various tissues, including the liver, kidneys, lungs, and intestines, and are classified into several families based on their structure and function.

Abnormalities in GST activity have been associated with increased susceptibility to certain diseases, such as cancer, neurological disorders, and respiratory diseases. Therefore, GSTs have become a subject of interest in toxicology, pharmacology, and clinical research.

Agaricales is an order of fungi that includes mushrooms, toadstools, and other gilled fungi. These fungi are characterized by their distinctive fruiting bodies, which have a cap (pileus) and stem (stipe), and gills (lamellae) on the underside of the cap where the spores are produced. Agaricales contains many well-known and economically important genera, such as Agaricus (which includes the common button mushroom), Amanita (which includes the deadly "death cap" mushroom), and Coprinus (which includes the inky cap mushrooms). The order was established by the Swedish mycologist Elias Magnus Fries in 1821.

Tert-butylhydroperoxide (t-BuOOH) is not typically considered a medical term, but rather a chemical compound. It is used in some medical and laboratory contexts. Here's a definition:

Tert-butylhydroperoxide (t-BuOOH) is an organic peroxide with the formula (CH3)3COOH. It is a colorless liquid, commercially available in concentrations up to 70%. It is used as an initiator in chemical reactions, a source of hydroxyl radicals in free-radical chemistry, and as a reagent in organic synthesis. Its use in medical contexts is typically limited to laboratory research and not as a therapeutic agent.

Handling tert-butylhydroperoxide requires caution due to its potential to cause fires and explosions when it comes into contact with certain substances, especially reducing agents and strong acids. Always follow safety guidelines and use appropriate personal protective equipment when handling this compound.

'Armoracia' is the genus name for a type of plant commonly known as horseradish. It belongs to the family Brassicaceae, which also includes vegetables such as broccoli, cabbage, and mustard greens. The root of the horseradish plant is used as a spice or condiment due to its pungent flavor, which is caused by the release of volatile oils when the root is grated or crushed.

Horseradish has been used in traditional medicine for various purposes, such as treating respiratory infections and promoting digestion. However, it is important to note that while some studies suggest potential health benefits of horseradish, more research is needed to confirm its effectiveness and safety. As with any medication or supplement, it is recommended to consult with a healthcare professional before using horseradish for medicinal purposes.

Thyroglobulin is a protein produced and used by the thyroid gland in the production of thyroid hormones, primarily thyroxine (T4) and triiodothyronine (T3). It is composed of two subunits, an alpha and a beta or gamma unit, which bind iodine atoms necessary for the synthesis of the thyroid hormones. Thyroglobulin is exclusively produced by the follicular cells of the thyroid gland.

In clinical practice, measuring thyroglobulin levels in the blood can be useful as a tumor marker for monitoring treatment and detecting recurrence of thyroid cancer, particularly in patients with differentiated thyroid cancer (papillary or follicular) who have had their thyroid gland removed. However, it is important to note that thyroglobulin is not specific to thyroid tissue and can be produced by some non-thyroidal cells under certain conditions, which may lead to false positive results in some cases.

Thiocyanates are chemical compounds that contain the thiocyanate ion (SCN-), which consists of a sulfur atom, a carbon atom, and a nitrogen atom. The thiocyanate ion is formed by the removal of a hydrogen ion from thiocyanic acid (HSCN). Thiocyanates are used in various applications, including pharmaceuticals, agrochemicals, and industrial chemicals. In medicine, thiocyanates have been studied for their potential effects on the thyroid gland and their use as a treatment for cyanide poisoning. However, excessive exposure to thiocyanates can be harmful and may cause symptoms such as irritation of the eyes, skin, and respiratory tract, as well as potential impacts on thyroid function.

Selenomethionine is an organic form of selenium, which is an essential trace element in human nutrition. It is incorporated into proteins in place of methionine, one of the 20 standard amino acids, and functions as an antioxidant by helping to prevent cellular damage from free radicals. Selenomethionine can be found in a variety of foods, including brazil nuts, fish, meat, and whole grains, and is also available as a dietary supplement.

Oxygen is a colorless, odorless, tasteless gas that constitutes about 21% of the earth's atmosphere. It is a crucial element for human and most living organisms as it is vital for respiration. Inhaled oxygen enters the lungs and binds to hemoglobin in red blood cells, which carries it to tissues throughout the body where it is used to convert nutrients into energy and carbon dioxide, a waste product that is exhaled.

Medically, supplemental oxygen therapy may be provided to patients with conditions such as chronic obstructive pulmonary disease (COPD), pneumonia, heart failure, or other medical conditions that impair the body's ability to extract sufficient oxygen from the air. Oxygen can be administered through various devices, including nasal cannulas, face masks, and ventilators.

Ferrocyanides are salts or complex ions containing the ferrocyanide ion (Fe(CN)2-4). The ferrocyanide ion is a stable, soluble, and brightly colored complex that contains iron in the +2 oxidation state coordinated to four cyanide ligands. Ferrocyanides are commonly used in various industrial applications such as water treatment, chemical synthesis, and photography due to their stability and reactivity. However, they can be toxic if ingested or inhaled in large quantities, so proper handling and disposal procedures should be followed.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

Medical definitions of "oxidants" refer to them as oxidizing agents or substances that can gain electrons and be reduced. They are capable of accepting electrons from other molecules in chemical reactions, leading to the production of oxidation products. In biological systems, oxidants play a crucial role in various cellular processes such as energy production and immune responses. However, an imbalance between oxidant and antioxidant levels can lead to a state of oxidative stress, which has been linked to several diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. Examples of oxidants include reactive oxygen species (ROS), such as superoxide anion, hydrogen peroxide, and hydroxyl radical, as well as reactive nitrogen species (RNS), such as nitric oxide and peroxynitrite.

The liver is a large, solid organ located in the upper right portion of the abdomen, beneath the diaphragm and above the stomach. It plays a vital role in several bodily functions, including:

1. Metabolism: The liver helps to metabolize carbohydrates, fats, and proteins from the food we eat into energy and nutrients that our bodies can use.
2. Detoxification: The liver detoxifies harmful substances in the body by breaking them down into less toxic forms or excreting them through bile.
3. Synthesis: The liver synthesizes important proteins, such as albumin and clotting factors, that are necessary for proper bodily function.
4. Storage: The liver stores glucose, vitamins, and minerals that can be released when the body needs them.
5. Bile production: The liver produces bile, a digestive juice that helps to break down fats in the small intestine.
6. Immune function: The liver plays a role in the immune system by filtering out bacteria and other harmful substances from the blood.

Overall, the liver is an essential organ that plays a critical role in maintaining overall health and well-being.

Phenols, also known as phenolic acids or phenol derivatives, are a class of chemical compounds consisting of a hydroxyl group (-OH) attached to an aromatic hydrocarbon ring. In the context of medicine and biology, phenols are often referred to as a type of antioxidant that can be found in various foods and plants.

Phenols have the ability to neutralize free radicals, which are unstable molecules that can cause damage to cells and contribute to the development of chronic diseases such as cancer, heart disease, and neurodegenerative disorders. Some common examples of phenolic compounds include gallic acid, caffeic acid, ferulic acid, and ellagic acid, among many others.

Phenols can also have various pharmacological activities, including anti-inflammatory, antimicrobial, and analgesic effects. However, some phenolic compounds can also be toxic or irritating to the body in high concentrations, so their use as therapeutic agents must be carefully monitored and controlled.

Laccase is an enzyme (specifically, a type of oxidoreductase) that is widely distributed in plants, fungi, and bacteria. It catalyzes the oxidation of various phenolic compounds, including polyphenols, methoxy-substituted phenols, aromatic amines, and some inorganic ions, while reducing molecular oxygen to water. This enzyme plays a crucial role in lignin degradation, as well as in the detoxification of xenobiotic compounds and in the synthesis of various pigments and polymers. The medical relevance of laccase is linked to its potential applications in bioremediation, biofuel production, and biotechnology.

Spectrum analysis in the context of Raman spectroscopy refers to the measurement and interpretation of the Raman scattering spectrum of a material or sample. Raman spectroscopy is a non-destructive analytical technique that uses the inelastic scattering of light to examine the vibrational modes of molecules.

When a monochromatic light source, typically a laser, illuminates a sample, a small fraction of the scattered light undergoes a shift in frequency due to interactions with the molecular vibrations of the sample. This shift in frequency is known as the Raman shift and is unique to each chemical bond or functional group within a molecule.

In a Raman spectrum, the intensity of the scattered light is plotted against the Raman shift, which is expressed in wavenumbers (cm-1). The resulting spectrum provides a "fingerprint" of the sample's molecular structure and composition, allowing for the identification and characterization of various chemical components within the sample.

Spectrum analysis in Raman spectroscopy can reveal valuable information about the sample's crystallinity, phase transitions, polymorphism, molecular orientation, and other properties. This technique is widely used across various fields, including materials science, chemistry, biology, pharmaceuticals, and forensics, to analyze a diverse range of samples, from simple liquids and solids to complex biological tissues and nanomaterials.

Pinocytosis is a type of cellular process involving the ingestion and absorption of extracellular fluid and dissolved substances into a cell. It is a form of endocytosis, where the cell membrane surrounds and engulfs the extracellular fluid to form a vesicle containing the fluid and its contents within the cell cytoplasm.

In pinocytosis, the cell membrane invaginates and forms small vesicles (pinocytotic vesicles) that contain extracellular fluid and dissolved substances. These vesicles then detach from the cell membrane and move into the cytoplasm, where they fuse with endosomes or lysosomes to break down and digest the contents of the vesicle.

Pinocytosis is a non-selective process that allows cells to take up small amounts of extracellular fluid and dissolved substances from their environment. It plays an important role in various physiological processes, including nutrient uptake, cell signaling, and the regulation of extracellular matrix composition.

Immunoenzyme techniques are a group of laboratory methods used in immunology and clinical chemistry that combine the specificity of antibody-antigen reactions with the sensitivity and amplification capabilities of enzyme reactions. These techniques are primarily used for the detection, quantitation, or identification of various analytes (such as proteins, hormones, drugs, viruses, or bacteria) in biological samples.

In immunoenzyme techniques, an enzyme is linked to an antibody or antigen, creating a conjugate. This conjugate then interacts with the target analyte in the sample, forming an immune complex. The presence and amount of this immune complex can be visualized or measured by detecting the enzymatic activity associated with it.

There are several types of immunoenzyme techniques, including:

1. Enzyme-linked Immunosorbent Assay (ELISA): A widely used method for detecting and quantifying various analytes in a sample. In ELISA, an enzyme is attached to either the capture antibody or the detection antibody. After the immune complex formation, a substrate is added that reacts with the enzyme, producing a colored product that can be measured spectrophotometrically.
2. Immunoblotting (Western blot): A method used for detecting specific proteins in a complex mixture, such as a protein extract from cells or tissues. In this technique, proteins are separated by gel electrophoresis and transferred to a membrane, where they are probed with an enzyme-conjugated antibody directed against the target protein.
3. Immunohistochemistry (IHC): A method used for detecting specific antigens in tissue sections or cells. In IHC, an enzyme-conjugated primary or secondary antibody is applied to the sample, and the presence of the antigen is visualized using a chromogenic substrate that produces a colored product at the site of the antigen-antibody interaction.
4. Immunofluorescence (IF): A method used for detecting specific antigens in cells or tissues by employing fluorophore-conjugated antibodies. The presence of the antigen is visualized using a fluorescence microscope.
5. Enzyme-linked immunosorbent assay (ELISA): A method used for detecting and quantifying specific antigens or antibodies in liquid samples, such as serum or culture supernatants. In ELISA, an enzyme-conjugated detection antibody is added after the immune complex formation, and a substrate is added that reacts with the enzyme to produce a colored product that can be measured spectrophotometrically.

These techniques are widely used in research and diagnostic laboratories for various applications, including protein characterization, disease diagnosis, and monitoring treatment responses.

Glutathione disulfide (GSSG) is the oxidized form of glutathione (GSH), which is a tripeptide composed of three amino acids: cysteine, glutamic acid, and glycine. It plays a crucial role in maintaining cellular redox homeostasis by scavenging free radicals and reactive oxygen species (ROS) in the body.

Glutathione exists in two forms - reduced (GSH) and oxidized (GSSG). In the reduced form, glutathione has a sulfhydryl group (-SH), which can donate an electron to neutralize free radicals and ROS. When glutathione donates an electron, it becomes oxidized and forms glutathione disulfide (GSSG).

Glutathione disulfide is a dimer of two glutathione molecules linked by a disulfide bond (-S-S-) between the sulfur atoms of their cysteine residues. The body can recycle GSSG back to its reduced form (GSH) through the action of an enzyme called glutathione reductase, which requires NADPH as a reducing agent.

Maintaining a proper balance between GSH and GSSG is essential for cellular health, as it helps regulate various physiological processes such as DNA synthesis, gene expression, immune function, and apoptosis (programmed cell death). An imbalance in glutathione homeostasis can lead to oxidative stress, inflammation, and the development of various diseases.

Anisoles are organic compounds that consist of a phenyl ring (a benzene ring with a hydroxyl group replaced by a hydrogen atom) attached to a methoxy group (-O-CH3). The molecular formula for anisole is C6H5OCH3. Anisoles are aromatic ethers and can be found in various natural sources, including anise plants and some essential oils. They have a wide range of applications, including as solvents, flavoring agents, and intermediates in the synthesis of other chemicals.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

Sodium Selenite is not a medical term per se, but it is a chemical compound with the formula Na2SeO3. It is used in medicine as a dietary supplement and also in veterinary medicine. Medically, it is used to treat selenium deficiency, which is rare.

Selenium is an essential trace element for human health, playing a crucial role in various physiological processes, such as antioxidant defense systems, thyroid hormone metabolism, and DNA synthesis. Sodium Selenite serves as a source of selenium in these medical applications.

Please note that supplementation with sodium selenite should be under the supervision of a healthcare professional, as excessive selenium intake can lead to selenosis, a condition characterized by symptoms like nausea, vomiting, hair loss, and neurological damage.

Amitrole is a non-selective herbicide that is used to control broadleaf weeds and some annual grasses. Its chemical name is 3-amino-1,2,4-triazole, and it works by inhibiting the enzyme responsible for the production of certain aromatic amino acids in plants, which are essential for their growth and development.

Amitrole is absorbed through the leaves and roots of plants and can be applied either before or after weed emergence. It is commonly used in agricultural settings, as well as in non-crop areas such as industrial sites, railways, and roadsides.

While amitrole is generally considered safe for use around humans and animals when used according to label instructions, it can cause eye and skin irritation, and may be harmful if swallowed or inhaled. It is important to follow all safety precautions when handling and applying this herbicide.

Erythrocytes, also known as red blood cells (RBCs), are the most common type of blood cell in circulating blood in mammals. They are responsible for transporting oxygen from the lungs to the body's tissues and carbon dioxide from the tissues to the lungs.

Erythrocytes are formed in the bone marrow and have a biconcave shape, which allows them to fold and bend easily as they pass through narrow blood vessels. They do not have a nucleus or mitochondria, which makes them more flexible but also limits their ability to reproduce or repair themselves.

In humans, erythrocytes are typically disc-shaped and measure about 7 micrometers in diameter. They contain the protein hemoglobin, which binds to oxygen and gives blood its red color. The lifespan of an erythrocyte is approximately 120 days, after which it is broken down in the liver and spleen.

Abnormalities in erythrocyte count or function can lead to various medical conditions, such as anemia, polycythemia, and sickle cell disease.

Benzene derivatives are chemical compounds that are derived from benzene, which is a simple aromatic hydrocarbon with the molecular formula C6H6. Benzene has a planar, hexagonal ring structure, and its derivatives are formed by replacing one or more of the hydrogen atoms in the benzene molecule with other functional groups.

Benzene derivatives have a wide range of applications in various industries, including pharmaceuticals, dyes, plastics, and explosives. Some common examples of benzene derivatives include toluene, xylene, phenol, aniline, and nitrobenzene. These compounds can have different physical and chemical properties depending on the nature and position of the substituents attached to the benzene ring.

It is important to note that some benzene derivatives are known to be toxic or carcinogenic, and their production, use, and disposal must be carefully regulated to ensure safety and protect public health.

Autoimmune thyroiditis, also known as Hashimoto's disease, is a chronic inflammation of the thyroid gland caused by an autoimmune response. In this condition, the immune system produces antibodies that attack and damage the thyroid gland, leading to hypothyroidism (underactive thyroid). The thyroid gland may become enlarged (goiter), and symptoms can include fatigue, weight gain, cold intolerance, constipation, dry skin, and depression. Autoimmune thyroiditis is more common in women than men and tends to run in families. It is often associated with other autoimmune disorders such as rheumatoid arthritis, Addison's disease, and type 1 diabetes. The diagnosis is typically made through blood tests that measure levels of thyroid hormones and antibodies. Treatment usually involves thyroid hormone replacement therapy to manage the symptoms of hypothyroidism.

I apologize for any confusion, but "plants" is not a term that has a medical definition. The term "plants" refers to a large and diverse group of organisms that obtain their energy through photosynthesis, which is the process of converting sunlight into chemical energy. Plants are typically characterized by having cells with cell walls containing cellulose, chloroplasts containing the pigment chlorophyll, and the ability to synthesize their own food through photosynthesis.

In a medical or biological context, you might be thinking of "plant-based" or "phytomedicine," which refer to the use of plants or plant extracts as a form of medicine or treatment. Phytomedicines have been used for thousands of years in many traditional systems of medicine, and some plant-derived compounds have been found to have therapeutic benefits in modern medicine as well. However, "plants" itself does not have a medical definition.

In medical terms, "bromides" refer to salts or compounds that contain bromine, a chemical element. Historically, potassium bromide was used as a sedative and anticonvulsant in the 19th and early 20th centuries. However, its use has largely been discontinued due to side effects such as neurotoxicity and kidney damage.

In modern medical language, "bromides" can also refer to something that is unoriginal, dull, or lacking in creativity, often used to describe ideas or expressions that are trite or clichéd. This usage comes from the fact that bromide salts were once commonly used as a sedative and were associated with a lack of excitement or energy.

Medical Definition of Vitamin E:

Vitamin E is a fat-soluble antioxidant that plays a crucial role in protecting your body's cells from damage caused by free radicals, which are unstable molecules produced when your body breaks down food or is exposed to environmental toxins like cigarette smoke and radiation. Vitamin E is also involved in immune function, DNA repair, and other metabolic processes.

It is a collective name for a group of eight fat-soluble compounds that include four tocopherols and four tocotrienols. Alpha-tocopherol is the most biologically active form of vitamin E in humans and is the one most commonly found in supplements.

Vitamin E deficiency is rare but can occur in people with certain genetic disorders or who cannot absorb fat properly. Symptoms of deficiency include nerve and muscle damage, loss of feeling in the arms and legs, muscle weakness, and vision problems.

Food sources of vitamin E include vegetable oils (such as sunflower, safflower, and wheat germ oil), nuts and seeds (like almonds, peanuts, and sunflower seeds), and fortified foods (such as cereals and some fruit juices).

Thioredoxins are a group of small proteins that contain a redox-active disulfide bond and play a crucial role in the redox regulation of cellular processes. They function as electron donors and help to maintain the intracellular reducing environment by reducing disulfide bonds in other proteins, thereby regulating their activity. Thioredoxins also have antioxidant properties and protect cells from oxidative stress by scavenging reactive oxygen species (ROS) and repairing oxidatively damaged proteins. They are widely distributed in various organisms, including bacteria, plants, and animals, and are involved in many physiological processes such as DNA synthesis, protein folding, and apoptosis.

I'm sorry for any confusion, but "Trametes" is not a medical term. It is a genus name in the fungal kingdom, specifically referring to a group of wood-decay fungi commonly known as "tough polypores." These fungi are often found growing on dead or dying trees and contribute to the decomposition process in natural ecosystems. They are not associated with human diseases or medical conditions.

High-performance liquid chromatography (HPLC) is a type of chromatography that separates and analyzes compounds based on their interactions with a stationary phase and a mobile phase under high pressure. The mobile phase, which can be a gas or liquid, carries the sample mixture through a column containing the stationary phase.

In HPLC, the mobile phase is a liquid, and it is pumped through the column at high pressures (up to several hundred atmospheres) to achieve faster separation times and better resolution than other types of liquid chromatography. The stationary phase can be a solid or a liquid supported on a solid, and it interacts differently with each component in the sample mixture, causing them to separate as they travel through the column.

HPLC is widely used in analytical chemistry, pharmaceuticals, biotechnology, and other fields to separate, identify, and quantify compounds present in complex mixtures. It can be used to analyze a wide range of substances, including drugs, hormones, vitamins, pigments, flavors, and pollutants. HPLC is also used in the preparation of pure samples for further study or use.

Organoselenium compounds are organic chemicals that contain selenium, a naturally occurring non-metal element, in their structure. Selenium is chemically related to sulfur and can replace it in many organic molecules. Organoselenium compounds have been studied for their potential therapeutic benefits, including antioxidant, anti-cancer, and anti-inflammatory effects. They are also used as catalysts in chemical reactions. These compounds contain at least one carbon atom bonded to selenium, which can take the form of a variety of functional groups such as selenoethers, selenols, and selenoesters.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Thioredoxin-disulfide reductase (Txnrd, TrxR) is an enzyme that belongs to the pyridine nucleotide-disulfide oxidoreductase family. It plays a crucial role in maintaining the intracellular redox balance by reducing disulfide bonds in proteins and keeping them in their reduced state. This enzyme utilizes NADPH as an electron donor to reduce thioredoxin (Trx), which then transfers its electrons to various target proteins, thereby regulating their activity, protein folding, and antioxidant defense mechanisms.

Txnrd is essential for several cellular processes, including DNA synthesis, gene expression, signal transduction, and protection against oxidative stress. Dysregulation of Txnrd has been implicated in various pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders. Therefore, understanding the function and regulation of this enzyme is of great interest for developing novel therapeutic strategies.

I'm sorry for any confusion, but there seems to be a mistake in your question. Prostaglandins are a group of lipid compounds that are synthesized in the body from fatty acids and have diverse hormonal-like effects in the body. They are not typically classified by a letter "G."

Prostaglandin G is an intermediate compound formed during the conversion of arachidonic acid to prostaglandins through the cyclooxygenase pathway. It is not a type or subclass of prostaglandins that has distinct medical relevance or definition. Therefore, I'm unable to provide a specific medical definition for 'Prostaglandins G.'

If you have any other questions or need clarification on a different topic, please let me know!

I'm sorry for any confusion, but "spectrum analysis" is not a commonly used medical term. Spectrum analysis is a term that is more frequently used in the fields of physics, mathematics, and engineering to describe the process of breaking down a signal or a wave into its different frequencies and amplitudes, creating a visual representation called a spectrum.

If you have any concerns about a medical issue, I would recommend consulting with a healthcare professional for accurate information and guidance.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

A chemical model is a simplified representation or description of a chemical system, based on the laws of chemistry and physics. It is used to explain and predict the behavior of chemicals and chemical reactions. Chemical models can take many forms, including mathematical equations, diagrams, and computer simulations. They are often used in research, education, and industry to understand complex chemical processes and develop new products and technologies.

For example, a chemical model might be used to describe the way that atoms and molecules interact in a particular reaction, or to predict the properties of a new material. Chemical models can also be used to study the behavior of chemicals at the molecular level, such as how they bind to each other or how they are affected by changes in temperature or pressure.

It is important to note that chemical models are simplifications of reality and may not always accurately represent every aspect of a chemical system. They should be used with caution and validated against experimental data whenever possible.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Sulfhydryl compounds, also known as thiol compounds, are organic compounds that contain a functional group consisting of a sulfur atom bonded to a hydrogen atom (-SH). This functional group is also called a sulfhydryl group. Sulfhydryl compounds can be found in various biological systems and play important roles in maintaining the structure and function of proteins, enzymes, and other biomolecules. They can also act as antioxidants and help protect cells from damage caused by reactive oxygen species. Examples of sulfhydryl compounds include cysteine, glutathione, and coenzyme A.

"Plant proteins" refer to the proteins that are derived from plant sources. These can include proteins from legumes such as beans, lentils, and peas, as well as proteins from grains like wheat, rice, and corn. Other sources of plant proteins include nuts, seeds, and vegetables.

Plant proteins are made up of individual amino acids, which are the building blocks of protein. While animal-based proteins typically contain all of the essential amino acids that the body needs to function properly, many plant-based proteins may be lacking in one or more of these essential amino acids. However, by consuming a variety of plant-based foods throughout the day, it is possible to get all of the essential amino acids that the body needs from plant sources alone.

Plant proteins are often lower in calories and saturated fat than animal proteins, making them a popular choice for those following a vegetarian or vegan diet, as well as those looking to maintain a healthy weight or reduce their risk of chronic diseases such as heart disease and cancer. Additionally, plant proteins have been shown to have a number of health benefits, including improving gut health, reducing inflammation, and supporting muscle growth and repair.

I believe there may be a slight misunderstanding in your question. "Plant leaves" are not a medical term, but rather a general biological term referring to a specific organ found in plants.

Leaves are organs that are typically flat and broad, and they are the primary site of photosynthesis in most plants. They are usually green due to the presence of chlorophyll, which is essential for capturing sunlight and converting it into chemical energy through photosynthesis.

While leaves do not have a direct medical definition, understanding their structure and function can be important in various medical fields, such as pharmacognosy (the study of medicinal plants) or environmental health. For example, certain plant leaves may contain bioactive compounds that have therapeutic potential, while others may produce allergens or toxins that can impact human health.

Phenylhydrazines are organic compounds that contain a phenyl group (a benzene ring with a hydrogen atom substituted by a hydroxy group) and a hydrazine group (-NH-NH2). They are aromatic amines that have been used in various chemical reactions, including the formation of azos and hydrazones. In medicine, phenylhydrazines were once used as vasodilators to treat angina pectoris, but their use has largely been discontinued due to their toxicity and potential carcinogenicity.

An Asparagus plant, scientifically known as *Asparagus officinalis*, is a perennial vegetable that belongs to the family *Asparagaceae*. It is native to Europe and western Asia. The plant is characterized by its long, thin green spears that grow out of the ground. These spears are harvested and eaten as a spring vegetable. The plant also produces fern-like foliage and small red berries. Asparagus is rich in nutrients, including fiber, vitamin C, vitamin A, and folate. It is also a good source of antioxidants.

In the field of medicine, "time factors" refer to the duration of symptoms or time elapsed since the onset of a medical condition, which can have significant implications for diagnosis and treatment. Understanding time factors is crucial in determining the progression of a disease, evaluating the effectiveness of treatments, and making critical decisions regarding patient care.

For example, in stroke management, "time is brain," meaning that rapid intervention within a specific time frame (usually within 4.5 hours) is essential to administering tissue plasminogen activator (tPA), a clot-busting drug that can minimize brain damage and improve patient outcomes. Similarly, in trauma care, the "golden hour" concept emphasizes the importance of providing definitive care within the first 60 minutes after injury to increase survival rates and reduce morbidity.

Time factors also play a role in monitoring the progression of chronic conditions like diabetes or heart disease, where regular follow-ups and assessments help determine appropriate treatment adjustments and prevent complications. In infectious diseases, time factors are crucial for initiating antibiotic therapy and identifying potential outbreaks to control their spread.

Overall, "time factors" encompass the significance of recognizing and acting promptly in various medical scenarios to optimize patient outcomes and provide effective care.

Coumaric acids are a type of phenolic acid that are widely distributed in plants. They are found in various foods such as fruits, vegetables, and grains. The most common forms of coumaric acids are p-coumaric acid, o-coumaric acid, and m-coumaric acid.

Coumaric acids have been studied for their potential health benefits, including their antioxidant, anti-inflammatory, and antimicrobial properties. They may also play a role in preventing chronic diseases such as cancer and cardiovascular disease. However, more research is needed to fully understand the potential health benefits of coumaric acids.

It's worth noting that coumaric acids are not to be confused with warfarin (also known as Coumadin), a medication used as an anticoagulant. While both coumaric acids and warfarin contain a similar chemical structure, they have different effects on the body.

Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.

In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.

Phenol, also known as carbolic acid, is an organic compound with the molecular formula C6H5OH. It is a white crystalline solid that is slightly soluble in water and has a melting point of 40-42°C. Phenol is a weak acid, but it is quite reactive and can be converted into a variety of other chemicals.

In a medical context, phenol is most commonly used as a disinfectant and antiseptic. It has a characteristic odor that is often described as "tarry" or " medicinal." Phenol is also used in some over-the-counter products, such as mouthwashes and throat lozenges, to help kill bacteria and freshen breath.

However, phenol is also a toxic substance that can cause serious harm if it is swallowed, inhaled, or absorbed through the skin. It can cause irritation and burns to the eyes, skin, and mucous membranes, and it can damage the liver and kidneys if ingested. Long-term exposure to phenol has been linked to an increased risk of cancer.

Because of its potential for harm, phenol is regulated as a hazardous substance in many countries, and it must be handled with care when used in medical or industrial settings.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Gene expression regulation, enzymologic refers to the biochemical processes and mechanisms that control the transcription and translation of specific genes into functional proteins or enzymes. This regulation is achieved through various enzymatic activities that can either activate or repress gene expression at different levels, such as chromatin remodeling, transcription factor activation, mRNA processing, and protein degradation.

Enzymologic regulation of gene expression involves the action of specific enzymes that catalyze chemical reactions involved in these processes. For example, histone-modifying enzymes can alter the structure of chromatin to make genes more or less accessible for transcription, while RNA polymerase and its associated factors are responsible for transcribing DNA into mRNA. Additionally, various enzymes are involved in post-transcriptional modifications of mRNA, such as splicing, capping, and tailing, which can affect the stability and translation of the transcript.

Overall, the enzymologic regulation of gene expression is a complex and dynamic process that allows cells to respond to changes in their environment and maintain proper physiological function.

Sodium azide is a chemical compound with the formula NaN3. Medically, it is not used as a treatment, but it can be found in some pharmaceutical and laboratory settings. It is a white crystalline powder that is highly soluble in water and has a relatively low melting point.

Sodium azide is well known for its ability to release nitrogen gas upon decomposition, which makes it useful as a propellant in airbags and as a preservative in laboratory settings to prevent bacterial growth. However, this property also makes it highly toxic to both animals and humans if ingested or inhaled, as it can cause rapid respiratory failure due to the release of nitrogen gas in the body. Therefore, it should be handled with great care and appropriate safety measures.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Diiodotyrosine (DIT) is a thyroid hormone precursor that contains two iodine atoms and the amino acid tyrosine. It is formed in the thyroid gland by the enzymatic iodination of tyrosine residues within the thyroglobulin protein. DIT can then be further combined and processed to form the active thyroid hormones triiodothyronine (T3) and thyroxine (T4), which contain three and four iodine atoms, respectively.

In summary, Diiodotyrosine is an essential intermediate in the synthesis of thyroid hormones T3 and T4.

'Staining and labeling' are techniques commonly used in pathology, histology, cytology, and molecular biology to highlight or identify specific components or structures within tissues, cells, or molecules. These methods enable researchers and medical professionals to visualize and analyze the distribution, localization, and interaction of biological entities, contributing to a better understanding of diseases, cellular processes, and potential therapeutic targets.

Medical definitions for 'staining' and 'labeling' are as follows:

1. Staining: A process that involves applying dyes or stains to tissues, cells, or molecules to enhance their contrast and reveal specific structures or components. Stains can be categorized into basic stains (which highlight acidic structures) and acidic stains (which highlight basic structures). Common staining techniques include Hematoxylin and Eosin (H&E), which differentiates cell nuclei from the surrounding cytoplasm and extracellular matrix; special stains, such as PAS (Periodic Acid-Schiff) for carbohydrates or Masson's trichrome for collagen fibers; and immunostains, which use antibodies to target specific proteins.
2. Labeling: A process that involves attaching a detectable marker or tag to a molecule of interest, allowing its identification, quantification, or tracking within a biological system. Labels can be direct, where the marker is directly conjugated to the targeting molecule, or indirect, where an intermediate linker molecule is used to attach the label to the target. Common labeling techniques include fluorescent labels (such as FITC, TRITC, or Alexa Fluor), enzymatic labels (such as horseradish peroxidase or alkaline phosphatase), and radioactive labels (such as ³²P or ¹⁴C). Labeling is often used in conjunction with staining techniques to enhance the specificity and sensitivity of detection.

Together, staining and labeling provide valuable tools for medical research, diagnostics, and therapeutic development, offering insights into cellular and molecular processes that underlie health and disease.

Ascorbate peroxidase Chloride peroxidase Cytochrome c peroxidase Haloperoxidase Hemoprotein Immunoperoxidase Lactoperoxidase ... Haem-using haem peroxidase and the related animal heme-dependent peroxidases DyP-type peroxidase family Catalase some ... Peroxidases are sometimes used as histological markers. Cytochrome c peroxidase is used as a soluble, easily purified model for ... Peroxidases typically catalyze a reaction of the form: ROOR ′ + 2 e − electron donor + 2 H + → Peroxidase ROH + R ′ OH {\ ...
... peroxidases, exhibiting both peroxidase and catalase activities. It is thought that catalase-peroxidase provides protection to ... Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to ... Another family of haem peroxidases is the DyP-type peroxidase family. Nelson RE, Fessler LI, Takagi Y, Blumberg B, Keene DR, ... Class II consists of secretory fungal peroxidases: ligninases, or lignin peroxidases (LiPs), and manganese-dependent ...
... , also called thyroperoxidase (TPO), thyroid specific peroxidase or iodide peroxidase, is an enzyme expressed ... Thyroid+Peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (CS1: long volume ... Thyroid peroxidase oxidizes iodide ions to form iodine atoms for addition onto tyrosine residues on thyroglobulin for the ... Thyroid peroxidase is a frequent epitope of autoantibodies in autoimmune thyroid disease, with such antibodies being called ...
... at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.11.1). ... Catalase-peroxidase (EC 1.11.1.21, katG (gene)) is an enzyme with systematic name donor:hydrogen-peroxide oxidoreductase. This ... Hochman A, Goldberg I (April 1991). "Purification and characterization of a catalase-peroxidase and a typical catalase from the ... a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli". Journal of ...
... is ideal in many respects for these applications because it is smaller, more stable, and less expensive ... Horseradish peroxidase is also commonly used in techniques such as ELISA and Immunohistochemistry due to its monomeric nature ... Horseradish peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (CS1: long ... The enzyme horseradish peroxidase (HRP), found in the roots of horseradish, is used extensively in biochemistry applications. ...
Other names in common use include TPNH peroxidase, NADP peroxidase, nicotinamide adenine dinucleotide phosphate peroxidase, TPN ... peroxidase, triphosphopyridine nucleotide peroxidase, and NADPH2 peroxidase. Conn EE, Kraemer LM, Liu PN, Vennesland B (1952 ... In enzymology, a NADPH peroxidase (EC 1.11.1.2) is an enzyme that catalyzes the chemical reaction NADPH + H+ + H2O2 ⇌ {\ ... This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The ...
In enzymology, a lignin peroxidase (EC 1.11.1.14) is an enzyme that catalyzes the chemical reaction 1,2-bis(3,4-dimethoxyphenyl ... Doyle WA, Blodig W, Veitch NC, Piontek K, Smith AT (1998). "Two substrate interaction sites in lignin peroxidase revealed by ... This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases) and can ... Paszczynski A; Huynh VB; Crawford R (1986). "Comparison of ligninase-I and peroxidase-M2 from the white-rot fungus ...
... (GPx) (EC 1.11.1.9) is the general name of an enzyme family with peroxidase activity whose main ... Glutathione peroxidase was discovered in 1957 by Gordon C. Mills. Activity of glutathione peroxidase is measured ... Glutathione peroxidase 2 is an intestinal and extracellular enzyme, while glutathione peroxidase 3 is extracellular, especially ... Glutathione peroxidase 1 (GPx1) is the most abundant version, found in the cytoplasm of nearly all mammalian tissues, whose ...
... (EC 1.11.1.16, VP, hybrid peroxidase, polyvalent peroxidase) is an enzyme with systematic name reactive- ... a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase ... Versatile+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 1.11.1). ... Camarero S, Ruiz-Dueñas FJ, Sarkar S, Martínez MJ, Martínez AT (October 2000). "The cloning of a new peroxidase found in ...
... is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive ... Eosinophil+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Eosinophil peroxidase on ... Eosinophil peroxidase can be found in the primary (azurophilic) granules of human and mammalian leukocytes. Peroxidase ... Eosinophil peroxidase is secreted by eosinophil cells into the tissue at the site of infection. Activation of cells in the face ...
Although MnP, like other lignin peroxidases, is a Class II peroxidase, it has a similar tertiary structure to prokaryotic Class ... Other names in common use include peroxidase-M2, and Mn-dependent (NADH-oxidizing) peroxidase. It employs one cofactor, heme. ... The peroxidase structure favors Mn(III)-chelates over free Mn(III) ions. The Mn(III) chelate interacts with the active site to ... Manganese peroxidase (commonly referred to as MnP) was discovered in 1985 simultaneously by the research groups of Michael H. ...
... (EC 1.11.1.18, bromoperoxidase, haloperoxidase (ambiguous), eosinophil peroxidase) is a family of enzymes ... For example, eosinophil peroxidase appears to prefer bromide over chloride, yet is not considered a bromoperoxidase because it ... Bromide+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (Articles with ... Bromo peroxidases of red and brown marine algae (Rhodophyta and Phaeophyta) contain vanadate (vanadium bromoperoxidase). ...
... (EC 1.11.1.10) is a family of enzymes that catalyzes the chlorination of organic compounds. This enzyme ... Hager LP, Hollenberg PF, Rand-Meir T, Chiang R, Doubek D (1975). "Chemistry of peroxidase intermediates". Ann. N. Y. Acad. Sci ... This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptors (peroxidases). The ... Poulos TL, Sundaramoorthy M, Terner J (1995). "The crystal structure of chloroperoxidase: a heme peroxidase--cytochrome P450 ...
Cytochrome c peroxidase Manganese peroxidase Kelly GJ, Latzko E (December 1979). "Soluble ascorbate peroxidase: detection in ... Other names in common use include L-ascorbic acid peroxidase, L-ascorbic acid-specific peroxidase, ascorbate peroxidase, and ... Peroxidases have been classified into three types (class I, class II and class III): ascorbate peroxidases is a class I ... Ascorbate peroxidase (or L-ascorbate peroxidase, APX) (EC 1.11.1.11) is an enzyme that catalyzes the chemical reaction L- ...
Other names in common use include DPNH peroxidase, NAD peroxidase, diphosphopyridine nucleotide peroxidase, NADH-peroxidase, ... nicotinamide adenine dinucleotide peroxidase, and NADH2 peroxidase. The crystal structure of NADH peroxidase resembles ... NADH inhibits the peroxidase activity of the NADH peroxidase by converting the enzyme to an unstable intermediate. NAD+ behaves ... NADH peroxidase, Alkyl hydroperoxide reductase and Thiol peroxidase) in oxidative stress response, survival inside macrophages ...
Dye-decolorizing peroxidase (EC 1.11.1.19, DyP, DyP-type peroxidase) is an enzyme with systematic name Reactive-Blue-5:hydrogen ... Sugano Y (April 2009). "DyP-type peroxidases comprise a novel heme peroxidase family". Cellular and Molecular Life Sciences. 66 ... "A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase ... Dye+decolorizing+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology v t e (EC ...
Plant peroxidase such as horseradish peroxidase and pineapple peroxidase B have low lysine, tryptophan, and tyrosine contents ... Cytochrome c peroxidase, or CCP, is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing ... Cytochrome c peroxidase, maintained by the Kraut Research Group. The UniProt entry for yeast cytochrome c peroxidase. Portal: ... Ellfolk N (1967). "Cytochrome c peroxidase. 3. The amino acid composition of cytochrome c peroxidase of Baker's yeast". Acta ...
This enzyme is also called long chain fatty acid peroxidase. MARTIN RO, STUMPF PK (1959). "Fat metabolism in higher plants. XII ... In enzymology, a fatty-acid peroxidase (EC 1.11.1.3) is an enzyme that catalyzes the chemical reaction palmitate + 2 H2O2 ⇌ {\ ... This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptor (peroxidases). The ...
Glutathione+amide-dependent+peroxidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology ... Glutathione amide-dependent peroxidase (EC 1.11.1.17) is an enzyme with systematic name glutathione amide:hydrogen-peroxide ... Identification of a novel thiol peroxidase (Prx/Grx) fueled by glutathione amide redox cycling". The Journal of Biological ...
... phospholipid hydroperoxide glutathione peroxidase, hydroperoxide glutathione peroxidase, or glutathione peroxidase 4 (GPX4). ... This enzyme belongs to the family of oxidoreductases, to be specific those acting on a peroxide as acceptor (peroxidases). The ... In enzymology, a phospholipid-hydroperoxide glutathione peroxidase (EC 1.11.1.12) is an enzyme that catalyzes the chemical ... Other names in common use include peroxidation-inhibiting protein, PHGPX, peroxidation-inhibiting protein: peroxidase, ...
Haem peroxidases were originally divided into two superfamilies, namely, the animal peroxidases and the plant peroxidases ( ... The DyP (for dye de-colourising peroxidase) family constitutes a novel class of haem peroxidase. Because these enzymes were ... In molecular biology, the DyP-type peroxidase family is a family of haem peroxidase enzymes. ... represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases". J. Biol. Chem. 282 ( ...
In molecular biology, the di-haem cytochrome c peroxidase family is a group of distinct cytochrome c peroxidases (CCPs) that ... Similar to other cytochrome c peroxidases, they reduce hydrogen peroxide to water using c-type haem as an oxidizable substrate ... Fulop V, Ridout CJ, Greenwood C, Hajdu J (November 1995). "Crystal structure of the di-haem cytochrome c peroxidase from ...
... is a family of peroxidases. Peroxidases are found in bacteria, fungi, plants and animals. On ... eosinophil peroxidase (EPO); lactoperoxidase (LPO); thyroid peroxidase (TPO); prostaglandin H synthase (PGHS); and peroxidasin ... The peroxidase active site, which catalyzes the reduction of PGG2 to PGH2, is located on the other side of the molecule, at the ... Kimura S, Hong YS, Kotani T, Ohtaki S, Kikkawa F (1989). "Structure of the human thyroid peroxidase gene: comparison and ...
... thyroid peroxidase activity; and hormone release. TSHR is involved in regulating seasonal reproduction in vertebrates. Graves' ...
It was first limited to class III peroxidases (plant peroxidases) and was then expanded to include all possible haem and non- ... The majority of haem and non-haem peroxidase sequences can now be found in the PeroxiBase. The database is hosted by the Swiss ... Peroxidase sequences come from other general public databases (NCBI, TIGR, UniProt KnowledgeBase: all the databases used are ... haem peroxidase protein sequences. Many researchers and bioinformaticians from the University of Geneva joined their efforts to ...
PRSS7 Eosinophil peroxidase deficiency; 261500; EPX Epidermodysplasia verruciformis; 226400; TMC6 Epidermodysplasia ...
Enzyme kinetics Glutathione peroxidase Peroxidase Superoxide dismutase GRCh38: Ensembl release 89: ENSG00000121691 - Ensembl, ... "PeroxiBase - The peroxidase database". Swiss Institute of Bioinformatics. Archived from the original on 2008-10-13. Retrieved ... Maehly AC, Chance B (1954). "The assay of catalases and peroxidases". Methods of Biochemical Analysis. Vol. 1. pp. 357-424. doi ... contains catalases and peroxidases. To activate the noxious spray, the beetle mixes the contents of the two compartments, ...
... eosinophil peroxidase (EPO), thyroid peroxidase (TPO), and prostaglandin H synthase (PGHS). A heme cofactor is bound near the ... Lactoperoxidase is a peroxidase enzyme secreted from mammary, salivary and other mucosal glands including the lungs, bronchii ... Peroxidase-generated hypoiodous acid (HOI), hypoiodite and hypothiocyanite all destroy the herpes simplex virus and human ... Lactoperoxidase is a member of the heme peroxidase family of enzymes. In humans, lactoperoxidase is encoded by the LPO gene. ...
... catalyzed by the presence of a peroxidase (such as horseradish peroxidase). The hydrogen peroxide is itself produced by an ... "Peroxidases". In Ashok Pandey; Colin Webb; Carlos Ricardo Soccol; Christian Larroche (eds.). Enzyme technology. Springer. p. ...
Anti-thyroid peroxidase (anti-TPO) antibodies are specific for the autoantigen TPO, a 105 kDa glycoprotein that catalyses ... McLachlan SM, Rapoport B (2000). "Autoimmune response to the thyroid in humans: thyroid peroxidase--the common autoantigenic ... The most clinically relevant anti-thyroid autoantibodies are anti-thyroid peroxidase antibodies (anti-TPO antibodies, TPOAb), ... Taurog A (May 1999). "Molecular evolution of thyroid peroxidase". Biochimie. 81 (5): 557-62. doi:10.1016/S0300-9084(99)80110-2 ...
Ascorbate peroxidase Chloride peroxidase Cytochrome c peroxidase Haloperoxidase Hemoprotein Immunoperoxidase Lactoperoxidase ... Haem-using haem peroxidase and the related animal heme-dependent peroxidases DyP-type peroxidase family Catalase some ... Peroxidases are sometimes used as histological markers. Cytochrome c peroxidase is used as a soluble, easily purified model for ... Peroxidases typically catalyze a reaction of the form: ROOR ′ + 2 e − electron donor + 2 H + → Peroxidase ROH + R ′ OH {\ ...
Thyroid peroxidase is a type of protein (called an enzyme) that cells in the thyroid gland use to make thyroid hormone. If ... Thyroid peroxidase is a type of protein (called an enzyme) that cells in the thyroid gland use to make thyroid hormone. If ... Thyroid peroxidase is a type of protein (called an enzyme) that cells in the thyroid gland use to make thyroid hormone. If ... Thyroid peroxidase (TPO, antimicrosomal antibody, antithyroid microsomal antibody) antibody - blood. In: Chernecky CC, Berger ...
PEROXIDASE C1ACALCIUM IONPROTOPORPHYRIN IX CONTAINING FE
Peroxidases catalyze a wide variety of peroxide-dependent oxidations. Based on sequence alignments, heme peroxidases have been ... Peroxidases catalyze a wide variety of peroxide-dependent oxidations. Based on sequence alignments, heme peroxidases have been ... The crystal structure of peanut peroxidase.. Schuller, D.J., Ban, N., Huystee, R.B., McPherson, A., Poulos, T.L.. (1996) ... Crystal structures are available for peroxidases of classes I and II, but until now no structure has been determined for class ...
glutathione peroxidase 1. Names. GSHPx-1. cellular glutathione peroxidase. selenoprotein GPX1. NP_000572.2. *EC 1.11.1.9 ... GSH peroxidase contains one selenocysteine residue per .... * NM_001329455.2 → NP_001316384.1 glutathione peroxidase 1 isoform ... GSH_Peroxidase; Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of ... GPX1 glutathione peroxidase 1 [Homo sapiens] GPX1 glutathione peroxidase 1 [Homo sapiens]. Gene ID:2876 ...
One class of enzymes are known as peroxidase. Peroxidase catalyze the oxidation of a particular substrate by hydrogen peroxide ... Horseradish Peroxidase Lab Report. 1090 Words , 5 Pages. To catalyze a reaction, an enzyme will grab on (bind) to one or more ... Peroxidase Lab. 224 Words , 1 Pages. The purpose of this study is to investigate the effects of varying the concentration of ... It was hypothesized that the optimal pH for the enzyme was pH 7 while the 1.0 ml peroxidase would have the best reaction rate. ...
The thyroid peroxidase antibodies test can help doctors diagnose and monitor autoimmune conditions involving the thyroid gland ... What Are Thyroid Peroxidase Antibodies?. Thyroid peroxidase (TPO) is an enzyme made by the thyroid gland. The thyroid uses ... Why Are Thyroid Peroxidase Antibodies Tests Done?. Doctors order thyroid peroxidase antibodies tests:. *to diagnose and monitor ... A thyroid peroxidase antibodies test checks for antibodies made against the TPO. Antibodies (also called immunoglobulins) are ...
Protein target information for Glutathione peroxidase (pig). Find diseases associated with this biological target and compounds ...
... ein Modulator der Tumorangiogenese und Endothelintegrität Glutathion Peroxidase 4 (Gpx4). ein ... Glutathion Peroxidase 4, Gpx4, Tumorangiogenese, Oxidativer Stress, Endothelfunktion. Subjects:. 600 Technology, Medicine. 600 ... Wortmann, Markus (2015): Glutathion Peroxidase 4 (Gpx4): ein Modulator der Tumorangiogenese und Endothelintegrität. ...
The thyroid peroxidase antibodies test can help doctors diagnose and monitor autoimmune conditions involving the thyroid gland ... What Are Thyroid Peroxidase Antibodies?. Thyroid peroxidase (TPO) is an enzyme made by the thyroid gland. The thyroid uses ... Why Are Thyroid Peroxidase Antibodies Tests Done?. Doctors order thyroid peroxidase antibodies tests:. *to diagnose and monitor ... Blood Test: Thyroid Peroxidase Antibodies. What Is a Blood Test?. By taking and testing a small sample of a persons blood, ...
Peroxidase Enzyme Activity , Flinn Scientific
Peroxidase 4/GPX4 products for your research including Glutathione Peroxidase 4/GPX4 Small Molecules and Glutathione Peroxidase ... Glutathione Peroxidase 4/GPX4: Products. Glutathione Peroxidase 4 (GPX4; also known as PHGPx) is a monomeric, 21 kDa member of ... the glutathione peroxidase family of proteins. It is widely expressed and serves to both protect cell membranes from ...
Home / Products / ABC Kits / VECTASTAIN ABC (Avidin-Biotin Complex Kits) / VECTASTAIN® Elite® ABC-HRP Kit, Peroxidase (Rabbit ... The VECTASTAIN Elite ABC system is the most sensitive avidin/biotin-based peroxidase system and is approximately 5 times more ... We offer a choice of either peroxidase or alkaline phosphatase based VECTASTAIN ABC kit detection systems. Selection of which ...
The role of the glutathione peroxidase/reductase (GSH-Px/GSSG-Rd) enzyme system in protection from paracetamol toxicity was ... The role of the glutathione peroxidase/reductase (GSH-Px/GSSG-Rd) enzyme system in protection from paracetamol toxicity was ... A role for the glutathione peroxidase/reductase enzyme system in the protection from paracetamol toxicity in isolated mouse ...
Peroxidase enzyme system is routinely used in Immunohistochemistry (IHC) and Immunocytochemistry (ICC). ... After the peroxidase reaction, wash slide with buffer 5-7X, (this buffer should not contain any sodium azide because peroxidase ... Peroxidase enzyme system is routinely used in Immunohistochemistry (IHC) and Immunocytochemistry (ICC). This Peroxidase ... Peroxidase enzyme system is routinely used in Immunohistochemistry (IHC) and Immunocytochemistry (ICC). ...
1) Horseradish (Armoracia rusticana) peroxidase is used in detection systems with different substrates. The enzyme binds a ...
Check out how our product, TrueBlue™ Peroxidase Substrate 10 mL can help with research, development, validation, and lab ... KPL TrueBlue provides the most sensitive means available to detect peroxidase-labeled conjugates. Because of its high ...
Selenium and glutathione peroxidase (EC 1.11.1.9) in blood components of New Zealand women - Volume 69 Issue 2 ... Tarp, U., Hansen, J. C., Overvad, K., Thorling, E. B., Tarp, B. D. & Graudal, H. (1987). Glutathione peroxidase activity in ... Whanger, P. D., Beilstein, M. A., Thomson, C. D., Robinson, M. F. & Howe, M. (1988). Blood selenium and glutathione peroxidase ... Avissar, N., Whitin, J. C., Allen, P. Z., Palmer, L. S. & Cohen, H. J. (1989). Antihuman plasma glutathione peroxidase ...
p>Learn more about Horseradish Peroxidase (HRP) antibodies and antigens from Meridian Bioscience ... MAb to Horseradish Peroxidase. Monoclonal. Purified. Mouse. IgG1. EIA,LF,WB. MG. K11111M. SDS. COA. Request Sample. ...
Protein target information for Glutathione peroxidase (Bacteroides thetaiotaomicron VPI-5482). Find diseases associated with ...
"Glutathione Peroxidase" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical ... This graph shows the total number of publications written about "Glutathione Peroxidase" by people in this website by year, and ... Is the protein surrounding the active site critical for hydrogen peroxide reduction by selenoprotein glutathione peroxidase? An ... Below are the most recent publications written about "Glutathione Peroxidase" by people in Profiles. ...
The peroxidase with an optimum activity at 50 °C was reasonably stable at 70 °C. The enzyme was active in the pH range 5-11, ... Peroxidase and arabinogalactan protein as by-products during somatic embryo cultivation in air-lift bioreactor. Publication ... HomePublicationsPeroxidase and arabinogalactan protein as by-products during somatic embryo cultivation in air-lift bioreactor ... Apart from various hydrolases, a high level of peroxidase activity (32 200 U/ltre medium, with specific activity of 1.3417 U/μg ...
Thorpe, Gary Harold Gregory Henry (1986). Enhanced chemiluminescent assays for horseradish peroxidase and their application in ... The utility of enhanced chemiluminescent assays for horseradish peroxidase conjugates was demonstrated in a range of ... These reactions produce novel, enhanced chemiluminescent assays for horseradish peroxidase labels used in immunoassays. ... Certain 6-hydroxybenzothiazole and phenol derivatives enhance light emission from the horseradish peroxidase catalysed ...
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Results: Melatonin caused an increase in glutathione level, the activity of glutathione peroxidase as well as glutathione ... The effect of melatonin on glutathione and glutathione transferase and glutathione peroxidase activities in the mouse liver and ... Objectives: The changes in reduced glutathione (GSH), activity of glutathione transferase (GST) and glutathione peroxidase ( ...
3. P. E. Thomas, et al., An Improved Staining Procedure for the Detection of the Peroxidase Activity of Cytochrome p-450 on ... TMBZ is a chromogenic reagent utilized for peroxidase detection. It has been developed as an alternative to benzidine, which is ... 4. H. H. Liem, et al., Quantitative Determination of Hemoglobin and Cytochemical Staining for Peroxidase Using 3, 3 E 5, 5 ... in the presence of hydrogen peroxide and peroxidase. The structure of this bluish-green complex is thought to be a radical form ...
Women with glomerulonephritis had both a significantly greater prevalence of thyroid peroxidase antibodies (odds ratio 3.85, 95 ... Women with glomerulonephritis had both a significantly greater prevalence of thyroid peroxidase antibodies (odds ratio 3.85, 95 ... Women with glomerulonephritis had both a significantly greater prevalence of thyroid peroxidase antibodies (odds ratio 3.85, 95 ... Increased prevalence of thyroid peroxidase antibodies (TPO-Ab) in women with glomerulonephritis. *Mark ...
... peroxidase/HRP conjugated) from Gentaur Antibodies. Cat Number: G-AB-12620. USA, UK & Europe Distribution. ... Rabbit Anti-Chicken IgY++ (IgG) (H+L) (peroxidase/HRP conjugated) , G-AB-12657 ... Donkey Anti-Goat IgG (H+L) (peroxidase/HRP conjugated) , G-AB-12650 ... Mouse Anti-Rabbit IgG (H+L) (peroxidase/HRP conjugated) , G-AB-12653 ...
GPx4 in mammals and tryparedoxin peroxidases in trypanosomes, and can be induced at distinct subcellular membranes depending on ... Ferroptosis is an evolutionary ancient process that is counterbalanced by distant peroxidases, ...
  • For example, horseradish peroxidase can use a variety of organic compounds as electron donors and acceptors. (wikipedia.org)
  • Horseradish peroxidase has an accessible active site, and many compounds can reach the site of the reaction. (wikipedia.org)
  • For example, phenols, which are important pollutants, can be removed by enzyme-catalyzed polymerization using horseradish peroxidase. (wikipedia.org)
  • 1) Horseradish (Armoracia rusticana) peroxidase is used in detection systems with different substrates. (bspp.org.uk)
  • Certain 6-hydroxybenzothiazole and phenol derivatives enhance light emission from the horseradish peroxidase catalysed oxidation of cyclic diacyl hydrazides such as luminol. (bham.ac.uk)
  • These reactions produce novel, enhanced chemiluminescent assays for horseradish peroxidase labels used in immunoassays. (bham.ac.uk)
  • The utility of enhanced chemiluminescent assays for horseradish peroxidase conjugates was demonstrated in a range of immunoassays, both immunoextraction and competitive, in conjunction with a variety of solid supports such as plastic beads, tubes and microtitre plates. (bham.ac.uk)
  • Horseradish Peroxidase Conjugated Antibody, supplied by OriGene, used in various techniques. (bioz.com)
  • Goat Anti Mouse Igg Horseradish Peroxidase Conjugate, supplied by OriGene, used in various techniques. (bioz.com)
  • Here, we reported a new phenomenon-the enzymatic oxidation of a single layer of graphitic carbon by horseradish peroxidase (HRP). (cdc.gov)
  • What Are Thyroid Peroxidase Antibodies? (kidshealth.org)
  • Why Are Thyroid Peroxidase Antibodies Tests Done? (kidshealth.org)
  • If you have questions about the thyroid peroxidase antibodies test or what the results of the test mean, talk to your doctor. (kidshealth.org)
  • Women with glomerulonephritis had both a significantly greater prevalence of thyroid peroxidase antibodies (odds ratio 3.85, 95% confidence interval 1.04-14.3) and an increased prevalence of elevated serum TSH values (P = 0.007). (lu.se)
  • The Thyroid Profile consists of a battery of several tests for the measurement of thyroid function, including Total and Free Thyroxine, Total and Free Triiodothyronine, Thyroglobulin, Thyroglobulin Antibodies, Thyroid Peroxidase Antibodies, and Thyroid Stimulating Hormone. (cdc.gov)
  • ce {Peroxidase}}]{ROH}+R'OH}}} For many of these enzymes the optimal substrate is hydrogen peroxide, but others are more active with organic hydroperoxides such as lipid peroxides. (wikipedia.org)
  • Glutathione peroxidases use glutathione as an electron donor and are active with both hydrogen peroxide and organic hydroperoxide substrates. (wikipedia.org)
  • The protein encoded by this gene belongs to the glutathione peroxidase family, members of which catalyze the reduction of organic hydroperoxides and hydrogen peroxide (H2O2) by glutathione, and thereby protect cells against oxidative damage. (nih.gov)
  • Is the protein surrounding the active site critical for hydrogen peroxide reduction by selenoprotein glutathione peroxidase? (umassmed.edu)
  • Although the TMBZ solution is colorless, it turns bluish-green (λmax: 655 nm) in the presence of hydrogen peroxide and peroxidase. (dojindo.com)
  • The family of glutathione peroxidase enzymes (GPX) acts by catalyzing the conversion of hydrogen peroxide or hydroperoxides to water or corresponding alcohols, participating in enzymatic defense against damage caused by ROS. (ufrgs.br)
  • Peroxidase activity was measured with 4 different hydrogen donors (ferulic acid, caffeic acid, pyrocatechol and pyrogallol). (tubitak.gov.tr)
  • There is a third natural antioxidant enzyme called, glutathione peroxidase which also reduces hydrogen peroxide to water. (yourdictionary.com)
  • X-ray crystallography, kinetics, spectroscopy and directed evolution have been used to define substrate binding in recombinant soybean cystolic ascorbate peroxidase (rsAPX), which catalyses the hydrogen peroxide-dependent oxidation of ascorbate in plants. (le.ac.uk)
  • The hydrogen peroxide produced is then scavenged by catalase and a variety of peroxidases. (prometheusprotocols.net)
  • Y. Nakano, K. Asada, Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts, Plant Cell Physiol. (prometheusprotocols.net)
  • Based on sequence alignments, heme peroxidases have been divided into three classes. (rcsb.org)
  • Collectively, the data show that all three members of the class I heme peroxidases can support radical formation on the distal tryptophan and that the reactivity of this radical can be controlled either by the protein structure or by the nature of the compound I intermediate. (bris.ac.uk)
  • Protonation of the proximal histidine ligand in heme peroxidases. (lu.se)
  • Ascorbate peroxidase (APX), cytochrome c peroxidase (CcP), and the catalase - peroxidases (KatG) share very similar active site structures and are distinguished from other peroxidases by the presence of a distal tryptophan residue. (bris.ac.uk)
  • The redox-sensitive transcription factor RAP2.4a mediates chloroplast-to-nucleus redox signaling and controls induction of the three most prominent chloroplast peroxidases, namely 2-Cys peroxiredoxin A (2CPA) and thylakoid- and stromal ascorbate peroxidase (tAPx and sAPx). (fu-berlin.de)
  • Usually, the immune system doesn't make a lot of antibodies against thyroid peroxidase because it's not a germ. (kidshealth.org)
  • positive titers of antibodies against thyroid peroxidase was the main underlying abnormality found in 16 out of 27 (59.2%) of patients with DEMS/SAPS compared to 11 out of 54 (20.4%) of pSS controls (p = 0.0009). (vitality101.com)
  • The thyroid peroxidase antibody test measures these antibodies in the blood. (medlineplus.gov)
  • Thyroid peroxidase (TPO, antimicrosomal antibody, antithyroid microsomal antibody) antibody - blood. (medlineplus.gov)
  • Donkey IgG F(ab')2 fragment Peroxidase conjugated secondary antibody reagents are ideal for ELISA, western blotting, Immunohistochemistry, Fluorescence Microscopy, Flow Cytometry as well as other antibody detection methods. (rockland.com)
  • On the other hand, for an enzyme such as cytochrome c peroxidase, the compounds that donate electrons are very specific, due to a very narrow active site. (wikipedia.org)
  • Protein families that serve as peroxidases include: Haem-using haem peroxidase and the related animal heme-dependent peroxidases DyP-type peroxidase family Catalase some haloperoxidase Di-haem cytochrome c peroxidase Non-heme Thiol: glutathione peroxidase, peroxiredoxin vanadium bromoperoxidase Alkyl hydroperoxide reductase Manganese peroxidase NADH peroxidase The glutathione peroxidase family consists of 8 known human isoforms. (wikipedia.org)
  • Cytochrome c peroxidase is used as a soluble, easily purified model for cytochrome c oxidase. (wikipedia.org)
  • An Improved Staining Procedure for the Detection of the Peroxidase Activity of Cytochrome p-450 on Sodium Dodecyl Sulfate Polyacrylamide Gels. (dojindo.com)
  • This structure provides new rationalization of the unusual functional features of the related cytochrome c peroxidase enzyme, and a mechanism for electron transfer from the substrate to the heme has been prepared (Chapter 3). (le.ac.uk)
  • Peroxidases (PRXs) and laccases (LACs) are enzymes involved in catalyzing the oxidation of the lignin monomers to facilitate lignin polymerization . (bvsalud.org)
  • Many members of the Solanaceae, notably Solanum melongena (eggplant/aubergine) and Capsicum chinense (the habanero/Scotch bonnet varieties of chili peppers) use Guaiacol and the enzyme guaiacol peroxidase as a defense against bacterial parasites such as Ralstonia solanacearum: the gene expression for this enzyme commences within minutes of bacterial attack. (wikipedia.org)
  • Prakasha, A, Umesha, S. Biochemical and Molecular Variations of Guaiacol Peroxidase and Total Phenols in Bacterial Wilt Pathogenesis of Solanum melongena. (wikipedia.org)
  • We have repeatedly observed that aqueous peroxide solutions do not quench thoroughly when large amounts of endogenous peroxidase are present. (utsouthwestern.edu)
  • Minute™ Peroxidase Suppressor is designed to inhibit endogenous peroxidase activity commonly encountered in immunohistochemistry (IHC) procedures. (biolinkk.com)
  • Inhibiting endogenous peroxidase activity is essential for avoiding false positives and reducing the background of IHC. (biolinkk.com)
  • Minute™ HRP Suppressor is a mixture of several potent HRP inhibitors and the result is a complete inhibition of endogenous peroxidase activity. (biolinkk.com)
  • Major Features: Very stable at RT, ready to use and irreversible inhibition of endogenous peroxidase activity. (biolinkk.com)
  • Wortmann, Markus (2015): Glutathion Peroxidase 4 (Gpx4): ein Modulator der Tumorangiogenese und Endothelintegrität. (uni-muenchen.de)
  • Glutathione Peroxidase 4/GPX4 " has 7 results in Products. (rndsystems.com)
  • The oxido-reductase enzyme glutathione peroxidase 4 (GPX4) governs Salmonella Typhimurium-induced neutrophil transepithelial migration. (umassmed.edu)
  • also known as PHGPx) is a monomeric, 21 kDa member of the glutathione peroxidase family of proteins. (rndsystems.com)
  • A majority of peroxidase protein sequences can be found in the PeroxiBase database. (wikipedia.org)
  • Thyroid peroxidase is a type of protein (called an enzyme) that cells in the thyroid gland use to make thyroid hormone. (medlineplus.gov)
  • Apart from various hydrolases, a high level of peroxidase activity (32 200 U/ltre medium, with specific activity of 1.3417 U/μg protein) has been obtained. (amrita.edu)
  • Consequences of genetic variations in the glutathione peroxidase 1 selenoprotein. (uic.edu)
  • This dosage induces optimum levels of the antioxidant enzyme glutathione peroxidase in the lungs. (yourdictionary.com)
  • The role of the glutathione peroxidase/reductase (GSH-Px/GSSG-Rd) enzyme system in protection from paracetamol toxicity was investigated in isolated mouse hepatocytes in primary culture. (nih.gov)
  • Peroxidase enzyme system is routinely used in Immunohistochemistry (IHC) and Immunocytochemistry (ICC). (immunochemistry.com)
  • For this purpose, the alkaline phosphatase product is identified by its cerium content via energy filtered transmission electron microscopy and thereby differentiated from cerium-free peroxidase-derived precipitates. (tu-berlin.de)
  • The activity of an enzyme (glutathione peroxidase ) in platelets (small blood cells essential in blood clotting) may be evaluated to assess selenium status. (yourdictionary.com)
  • After the peroxidase reaction, wash slide with buffer 5-7X, (this buffer should not contain any sodium azide because peroxidase is inactivated) and distilled/deionized water 2X. (immunochemistry.com)
  • The role of peroxidase and IAA oxidase activities in defense mechanisms in response to heavy metal toxicity is discussed. (tubitak.gov.tr)
  • Peroxidases catalyze a wide variety of peroxide-dependent oxidations. (rcsb.org)
  • 1989. Polymerization of substituted anilines, phenols, and heterocyclic compounds by peroxidase in organic solvents. (wikipedia.org)
  • Resonance Raman (RR) spectra of several compounds III of lignin peroxidase (LiP) have been measured at 90 K with Soret and visible excitation wavelengths. (elsevierpure.com)
  • Glutathione Peroxidase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
  • Análise da expressão dos genes de glutationa peroxidase em arroz (Oryza sativa L. (ufrgs.br)
  • Além disso, foi obtida uma construção para transformação de arroz, contendo os genes repórteres GUS e GFP, a fim de realizar o estudo do promotor do gene da Glutationa Peroxidase 3. (ufrgs.br)
  • In addition, it was obtained a construct for transformation of rice, containing the GUS and GFP reporter genes in order to study the Glutathione Peroxidase 3 gene promoter. (ufrgs.br)
  • This Peroxidase Enhancing system increases the level of sensitivity in peroxidase based chromogens (AEC and DAB). (immunochemistry.com)
  • Other studies have shown that peroxidases may be used successfully to polymerize anilines and phenols in organic solvent matrices. (wikipedia.org)
  • Iodine, ingested in food and water as iodide, is actively concentrated by the thyroid and converted to organic iodine (organification) within follicular cells by thyroid peroxidase. (msdmanuals.com)
  • To extend available double labeling procedures such as combinations of immunogold and peroxidase methods, an additional, gold- and peroxidase-independent procedure would represent a considerable advantage. (tu-berlin.de)
  • We offer a choice of either peroxidase or alkaline phosphatase based VECTASTAIN ABC kit detection systems. (vectorlabs.com)
  • The peroxidase with an optimum activity at 50 °C was reasonably stable at 70 °C. The enzyme was active in the pH range 5-11, with an optimum at pH 6. (amrita.edu)
  • Phylogenetic analysis reveals that HPX15, AsP-15 and AcP-15 are unique to Anophelines and this may be due to the involvement of this peroxidase in regulation of Plasmodium development. (biomedcentral.com)
  • There are many investigations about the use of peroxidase in many manufacturing processes like adhesives, computer chips, car parts, and linings of drums and cans. (wikipedia.org)