An enzyme that catalyzes the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. EC
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.
Inorganic compounds derived from hydrochloric acid that contain the Cl- ion.
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
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
A hemeprotein which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. EC
Cell membrane glycoproteins that form channels to selectively pass chloride ions. Nonselective blockers include FENAMATES; ETHACRYNIC ACID; and TAMOXIFEN.
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
A gas that has been used as an aerosol propellant and is the starting material for polyvinyl resins. Toxicity studies have shown various adverse effects, particularly the occurrence of liver neoplasms.
A ubiquitous sodium salt that is commonly used to season food.
A polyvinyl resin used extensively in the manufacture of plastics, including medical devices, tubing, and other packaging. It is also used as a rubber substitute.
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.
Mercury chloride (HgCl2). A highly toxic compound that volatizes slightly at ordinary temperature and appreciably at 100 degrees C. It is corrosive to mucous membranes and used as a topical antiseptic and disinfectant.
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.

Heterologous expression of the vanadium-containing chloroperoxidase from Curvularia inaequalis in Saccharomyces cerevisiae and site-directed mutagenesis of the active site residues His(496), Lys(353), Arg(360), and Arg(490). (1/107)

The vanadium-containing chloroperoxidase from the fungus Curvularia inaequalis is heterologously expressed to high levels in the yeast Saccharomyces cerevisiae. Characterization of the recombinant enzyme reveals that this behaves very similar to the native chloroperoxidase. Site-directed mutagenesis is performed on four highly conserved active site residues to examine their role in catalysis. When the vanadate-binding residue His(496) is changed into an alanine, the mutant enzyme loses the ability to bind vanadate covalently resulting in an inactive enzyme. The negative charges on the vanadate oxygens are compensated by hydrogen bonds with the residues Arg(360), Arg(490), and Lys(353). When these residues are changed into alanines the mutant enzymes lose the ability to effectively oxidize chloride but can still function as bromoperoxidases. A general mechanism for haloperoxidase catalysis is proposed that also correlates the kinetic properties of the mutants with the charge and the hydrogen-bonding network in the vanadate-binding site.  (+info)

Striking activation of oxidative enzymes suspended in nonaqueous media. (2/107)

The catalytic activity of four lyophilized oxidative enzymes-horseradish peroxidase, soybean peroxidase, Caldariomyces fumago chloroperoxidase, and mushroom polyphenol oxidase-is much lower when directly suspended in organic solvents containing little water than when they are introduced into the same largely nonaqueous media by first dissolving them in water and then diluting with anhydrous solvents. The lower the water content of the medium, the greater this discrepancy becomes. The mechanism of this phenomenon was found to arise from reversible denaturation of the oxidases on lyophilization: because of its conformational rigidity, the denatured enzyme exhibits very limited activity when directly suspended in largely nonaqueous media but renatures and thus yields much higher activity if first redissolved in water. Two independent means were discovered for dramatically minimizing the lyophilization-induced inactivation, both involving the addition of certain types of excipients to the aqueous enzyme solution before lyophilization. The first group of excipients consists of phenolic and aniline substrates as well as other hydrophobic compounds; these presumably bind to the hydrophobic pocket of the enzyme active site, thereby preventing its collapse during dehydration. The second group consists of general lyoprotectants such as polyols and polyethylen glycol that apparently preserve the overall enzyme structure during dehydration. The activation effects of such excipients can reach into the tens and hundreds of fold. Moreover, the activations afforded by the two excipient groups are additive, resulting in up to a complete protection against lyophilization-induced inactivation when representatives of the two are present together.  (+info)

Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue. (3/107)

Chloroperoxidase is a versatile heme enzyme which can cross over the catalytic boundaries of other oxidative hemoproteins and perform multiple functions. Chloroperoxidase, in addition to catalyzing classical peroxidative reactions, also acts as a P450 cytochrome and a potent catalase. The multiple functions of chloroperoxidase must be derived from its unique active site structure. Chloroperoxidase possesses a proximal cysteine thiolate heme iron ligand analogous to the P450 cytochromes; however, unlike the P450 enzymes, chloroperoxidase possesses a very polar environment distal to its heme prosthetic group and contains a glutamic acid residue in close proximity to the heme iron. The presence of a thiolate ligand in chloroperoxidase has long been thought to play an essential role in its chlorination and epoxidation activities; however, the research reported in this paper proves that hypothesis to be invalid. To explore the role of Cys-29, the amino acid residue supplying the thiolate ligand in chloroperoxidase, Cys-29 has been replaced with a histidine residue. Mutant clones of the chloroperoxidase genome have been expressed in a Caldariomyces fumago expression system by using gene replacement rather than gene insertion technology. C. fumago produces wild-type chloroperoxidase, thus requiring gene replacement of the wild type by the mutant gene. To the best of our knowledge, this is the first time that gene replacement has been reported for this type of fungus. The recombinant histidine mutants retain most of their chlorination, peroxidation, epoxidation, and catalase activities. These results downplay the importance of a thiolate ligand in chloroperoxidase and suggest that the distal environment of the heme active site plays the major role in maintaining the diverse activities of this enzyme.  (+info)

Peroxidase and phosphatase activity of active-site mutants of vanadium chloroperoxidase from the fungus Curvularia inaequalis. Implications for the catalytic mechanisms. (4/107)

Mutation studies were performed on active-site residues of vanadium chloroperoxidase from the fungus Curvularia inaequalis, an enzyme which exhibits both haloperoxidase and phosphatase activity and is related to glucose-6-phosphatase. The effects of mutation to alanine on haloperoxidase activity were studied for the proposed catalytic residue His-404 and for residue Asp-292, which is located close to the vanadate cofactor. The mutants were strongly impaired in their ability to oxidize chloride but still oxidized bromide, although they inactivate during turnover. The effects on the optical absorption spectrum of vanadium chloroperoxidase indicate that mutant H404A has a reduced affinity for the cofactor, whereas this affinity is unchanged in mutant D292A. The effect on the phosphatase activity of the apoenzyme was investigated for six mutants of putative catalytic residues. Effects of mutation of His-496, Arg-490, Arg-360, Lys-353, and His-404 to alanine are in line with their proposed roles in nucleophilic attack, transition-state stabilization, and leaving-group protonation. Asp-292 is excluded as the group that protonates the leaving group. A model based on the mutagenesis studies is presented and may serve as a template for glucose-6-phosphatase and other related phosphatases. Hydrolysis of a phospho-histidine intermediate is the rate-determining step in the phosphatase activity of apochloroperoxidase, as shown by burst kinetics.  (+info)

X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate. (5/107)

The structure of Escherichia blattae non-specific acid phosphatase (EB-NSAP) has been determined at 1.9 A resolution with a bound sulfate marking the phosphate-binding site. The enzyme is a 150 kDa homohexamer. EB-NSAP shares a conserved sequence motif not only with several lipid phosphatases and the mammalian glucose-6-phosphatases, but also with the vanadium-containing chloroperoxidase (CPO) of Curvularia inaequalis. Comparison of the crystal structures of EB-NSAP and CPO reveals striking similarity in the active site structures. In addition, the topology of the EB-NSAP core shows considerable similarity to the fold of the active site containing part of the monomeric 67 kDa CPO, despite the lack of further sequence identity. These two enzymes are apparently related by divergent evolution. We have also determined the crystal structure of EB-NSAP complexed with the transition-state analog molybdate. Structural comparison of the native enzyme and the enzyme-molybdate complex reveals that the side-chain of His150, a putative catalytic residue, moves toward the molybdate so that it forms a hydrogen bond with the metal oxyanion when the molybdenum forms a covalent bond with NE2 of His189.  (+info)

Prochiral selectivity in H(2)O(2)-promoted oxidation of arylalkanols catalysed by chloroperoxidase. The role of the interactions between the OH group and the amino-acid residues in the enzyme active site. (6/107)

The H(2)O(2)-promoted oxidations of (R)-[alpha-(2)H(1)]-and (S)-[alpha-(2)H(1)]-arylalkanols catalysed by chloroperoxidase (CPO) from Caldariomyces fumago have been investigated. It has been found that with (R)-[alpha-(2)H(1)]-alcohols, the oxidation involves almost exclusively the cleavage of the C-H bond, whereas in the case of the oxidation of (S)-[alpha-(2)H(1)]-alcohols, the C-D bond is preferentially broken. These results clearly indicate that the reactions of corresponding undeuterated arylalkanols are characterized by a high prochiral selectivity, involving the cleavage of the pro-S C-H bond. This prochiral selectivity is poorly influenced by the electronic effect of ring substituents, whereas it decreases with the length of the carbon lateral chain, in the order: benzyl alcohol > 2-phenylethanol > 3-phenylpropanol. Molecular binding studies showed that the main factor directing the docking of the substrate in such a specific orientation in the enzyme active site is the interaction between the alcoholic OH group and the residue Glu183. This interaction is likely to drive both the stereochemistry and the regiochemistry of these reactions. A bifurcated hydrogen bond involving the OH group, the carboxylate oxygen of Glu183 and the oxoferryl oxygen might also be operating.  (+info)

Expression of the Caldariomyces fumago chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme. (7/107)

The Caldariomyces fumago chloroperoxidase was successfully expressed in Aspergillus niger. The recombinant enzyme was produced in the culture medium as an active protein and could be purified by a three-step purification procedure. The catalytic behavior of recombinant chloroperoxidase (rCPO) was studied and compared with that of native CPO. The specific chlorination activity (47 units/nmol) of rCPO and its pH optimum (pH 2.75) were very similar to those of native CPO. rCPO catalyzes the oxidation of various substrates in comparable yields and selectivities to native CPO. Indole was oxidized to 2-oxindole with 99% selectivity and thioanisole to the corresponding R-sulfoxide (enantiomeric excess >98%). Incorporation of (18)O from labeled H(2)18O(2) into the oxidized products was 100% in both cases.  (+info)

Roles of water in heme peroxidase and catalase mechanisms. (8/107)

A water molecule is coproduced with the Compound I intermediate in the reactions of native heme peroxidases and catalases with hydrogen peroxide. As a result of water release/rebinding from/to the coproduct formation site the Compound I intermediate may exist in two forms: a "wet" form, Compound I(H(2)O), in which a water molecule is present at or near the site of coproduct water formation, and Compound I, in which the coproduct water formation site is "dry." It is postulated that the absence or presence of a water molecule at this site provides the structural basis for a redox pathway switching mechanism, such that the transition states for 2-electron equivalent reduction of Compound I intermediates are accessible in the dry form, but that in the wet form only 1-electron equivalent processes are possible, unless release of water can be stimulated. This concept provides the basis of a general mechanism in which the classical functional distinction between catalases and peroxidases, as well as the more complex behavior observed in halide oxidation and halogenation reactions, appear as particular cases in which variations in the degree of retention of water at the coproduct formation site influence Compound I reactivity.  (+info)

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.

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.

Chlorides are simple inorganic ions consisting of a single chlorine atom bonded to a single charged hydrogen ion (H+). Chloride is the most abundant anion (negatively charged ion) in the extracellular fluid in the human body. The normal range for chloride concentration in the blood is typically between 96-106 milliequivalents per liter (mEq/L).

Chlorides play a crucial role in maintaining electrical neutrality, acid-base balance, and osmotic pressure in the body. They are also essential for various physiological processes such as nerve impulse transmission, maintenance of membrane potentials, and digestion (as hydrochloric acid in the stomach).

Chloride levels can be affected by several factors, including diet, hydration status, kidney function, and certain medical conditions. Increased or decreased chloride levels can indicate various disorders, such as dehydration, kidney disease, Addison's disease, or diabetes insipidus. Therefore, monitoring chloride levels is essential for assessing a person's overall health and diagnosing potential medical issues.

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.

Chloride channels are membrane proteins that form hydrophilic pores or gaps, allowing the selective passage of chloride ions (Cl-) across the lipid bilayer of cell membranes. They play crucial roles in various physiological processes, including regulation of neuronal excitability, maintenance of resting membrane potential, fluid and electrolyte transport, and pH and volume regulation of cells.

Chloride channels can be categorized into several groups based on their structure, function, and mechanism of activation. Some of the major classes include:

1. Voltage-gated chloride channels (ClC): These channels are activated by changes in membrane potential and have a variety of functions, such as regulating neuronal excitability and transepithelial transport.
2. Ligand-gated chloride channels: These channels are activated by the binding of specific ligands or messenger molecules, like GABA (gamma-aminobutyric acid) or glycine, and are involved in neurotransmission and neuromodulation.
3. Cystic fibrosis transmembrane conductance regulator (CFTR): This is a chloride channel primarily located in the apical membrane of epithelial cells, responsible for secreting chloride ions and water to maintain proper hydration and mucociliary clearance in various organs, including the lungs and pancreas.
4. Calcium-activated chloride channels (CaCCs): These channels are activated by increased intracellular calcium concentrations and participate in various physiological processes, such as smooth muscle contraction, neurotransmitter release, and cell volume regulation.
5. Swelling-activated chloride channels (ClSwells): Also known as volume-regulated anion channels (VRACs), these channels are activated by cell swelling or osmotic stress and help regulate cell volume and ionic homeostasis.

Dysfunction of chloride channels has been implicated in various human diseases, such as cystic fibrosis, myotonia congenita, epilepsy, and certain forms of cancer.

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.

Vinyl Chloride is not a medical term, but rather a chemical compound. It's an organochloride with the formula C2H3Cl, and it's a colorless gas at room temperature that is used primarily in the production of polyvinyl chloride (PVC) plastics.

However, Vinyl Chloride is relevant to medical professionals because exposure to this compound has been linked to an increased risk of a rare form of liver cancer called hepatic angiosarcoma, as well as other health problems such as neurological damage and immune system suppression. Therefore, occupational exposure to Vinyl Chloride is regulated by organizations like the Occupational Safety and Health Administration (OSHA) in the United States.

Sodium Chloride is defined as the inorganic compound with the chemical formula NaCl, representing a 1:1 ratio of sodium and chloride ions. It is commonly known as table salt or halite, and it is used extensively in food seasoning and preservation due to its ability to enhance flavor and inhibit bacterial growth. In medicine, sodium chloride is used as a balanced electrolyte solution for rehydration and as a topical wound irrigant and antiseptic. It is also an essential component of the human body's fluid balance and nerve impulse transmission.

I'm sorry for any confusion, but "Polyvinyl Chloride" (PVC) is not a medical term. It is a type of synthetic plastic polymer material. PVC is commonly used in various industrial, commercial, and consumer products, such as pipes, cable insulation, clothing, and inflatable items.

If you have any medical concerns or questions, please provide them, and I would be happy to help you find a relevant answer.

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.

Mercuric chloride, also known as corrosive sublimate, is defined medically as a white or colorless crystalline compound used historically as a topical antiseptic and caustic. It has been used in the treatment of various skin conditions such as warts, thrush, and some parasitic infestations. However, its use is limited nowadays due to its high toxicity and potential for serious side effects, including kidney damage, digestive problems, and nervous system disorders. It is classified as a hazardous substance and should be handled with care.

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.

... (EC 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 ...
For example, although eosinophil peroxidase is able to oxidize chloride, it preferentially oxidizes bromide. The mammalian ... Horseradish peroxidase is also capable of oxidizing these substrates, but its heme is not covalently bound and becomes damaged ... Haloperoxidases are peroxidases that are able to mediate the oxidation of halides by hydrogen peroxide. Both halides and ... 264 (10): 5660 - Journal of Biological Chemistry [2] Role of Heme-Protein Covalent Bonds in Mammalian Peroxidases Winter, JM; ...
Hypobromite is produced via eosinophil peroxidase, an enzyme that can use chloride but preferentially uses bromide. The average ... see lithium chloride). Like lithium carbonate and lithium chloride, it was used as a treatment for bipolar disorder. From 1954 ... of those in blood and are strongly influenced by the body's chloride intake and metabolism. Since bromide is still used in ... its relationship to levels of both chloride and total dissolved solids and the implications for water treatment, Chemosphere, ...
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 {\ ...
For example, eosinophil peroxidase appears to prefer bromide over chloride, yet is not considered a bromoperoxidase because it ... Bromide peroxidase (EC, bromoperoxidase, haloperoxidase (ambiguous), eosinophil peroxidase) is a family of enzymes ... 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). ...
... chloride peroxidase MeSH D08.811.682.732.380 - cytochrome-c peroxidase MeSH D08.811.682.732.440 - eosinophil peroxidase MeSH ... iodide peroxidase MeSH D08.811.682.732.550 - lactoperoxidase MeSH D08.811.682.732.700 - peroxidase MeSH D08.811.682.810.567 - ... horseradish peroxidase MeSH D08.811.682.732.512.900 - wheat germ agglutinin-horseradish peroxidase conjugate MeSH D08.811. ... D08.811.682.732.500 - glutathione peroxidase MeSH D08.811.682.732.512 - ...
Chile Charge Point Operator installs and maintains charge stations Chloride peroxidase, an enzyme Classic Produktion Osnabrück ...
Eosinophil peroxidase is a haloperoxidase that preferentially uses bromide over chloride for this purpose, generating ... Conversely, the bromide ion is a weaker reducing agent than iodide, but a stronger one than chloride. These similarities led to ... Anhydrous hydrogen bromide is a poor solvent, only able to dissolve small molecular compounds such as nitrosyl chloride and ... For example, in the presence of hydrogen peroxide, H2O2, formed by the eosinophil, and either chloride or bromide ions, ...
... eosinophil peroxidase, important for defense against multicellular parasites, uses bromide ion in preference to chloride ion. 5 ... Even though the concentration of bromide is only 0.3% of that for chloride in sea water, organobromine compounds are more ...
EPO can take chloride, bromide and iodide as substrates, as well as the pseudohalide thiocyanate (SCN−). However, the enzyme ... Eosinophil peroxidase 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 ...
The chloride and bromide in ocean waters are the source of the halogens. Various peroxidase enzymes (e.g., bromoperoxidase ... Aryl chlorides are the aryl halides produced on the largest scale commercially: 150,000 tons/y in the US alone (1994). ... The most important members are the aryl chlorides, but the class of compounds is so broad that there are many derivatives and ... Owing to high cost of diazonium salts, this method is reserved for specialty chlorides. The main aryl bromides produced ...
These cells react the bromide with peroxide to generate hypobromite by the action of eosinophil peroxidase, a haloperoxidase ... enzyme which preferentially uses bromide over chloride for this purpose. Simple bromide salts (such as sodium bromide) are also ... in a similar fashion to the action of peroxidase on bromide in eosinophils. Hypobromite has been proposed to be a reactive ...
... (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is most abundantly ... and chloride anion (Cl−) (or hypobromous acid if Br- is present) during the neutrophil's respiratory burst. It requires heme as ... MPO is a member of the XPO subfamily of peroxidases and produces hypochlorous acid (HOCl) from hydrogen peroxide (H2O2) ...
In mammals, there are pathways for the metabolism of peroxides using various enzymes of the peroxidase class. For BTP, this ... The deactivation is carried out by adding anhydrous calcium chloride to the mixture. The deactivated mixture is scrubbed with ... would correspond to the following general reaction scheme:[citation needed] Peroxidase + C2F6O2 → 2CF3O− The peroxidase will ...
If streptavidin-HRP (streptavidin and horseradish peroxidase conjugate) is used, then using TMB (tetramethylbenzidine) as a ... a mixture of 5-bromo-4-chloro-3-indolyl phosphate and nitroblue tetrazolium chloride) as a substrate will produce more distinct ...
Iodide then travels from within the cell into the lumen, through the action of pendrin, an iodide-chloride antiporter. In the ... Antibodies against thyroid peroxidase can be found on testing. The inflammation usually resolves without treatment, although ... and the iodine is attached to the active tyrosine units in thyroglobulin by the enzyme thyroid peroxidase. This forms the ...
... and chloride, Cl−. Chlorite dismutase is a heme-containing protein, but it bears no structural or sequence relationships with ... known peroxidases or other heme proteins and is part of a large family of proteins with more than one biochemical function. ...
The chlorides are obtained by chlorination of the selenenyl chloride. Seleniranes are three-membered rings (parent: C2H4Se) ... They occur in some selenoenzymes, such as glutathione peroxidase. Seleninic acids (RSe(O)OH) are analogues of sulfinic acids. ...
... peroxidase EC iodide peroxidase EC glutathione peroxidase EC chloride peroxidase EC L ... NADH peroxidase EC NADPH peroxidase EC fatty-acid peroxidase EC Now EC EC ... versatile peroxidase EC glutathione amide-dependent peroxidase EC bromide peroxidase EC dye ... phospholipid-hydroperoxide glutathione peroxidase EC manganese peroxidase EC lignin peroxidase EC 1.11. ...
... l is one important characteristic of animal peroxidases; plant peroxidases incorporate heme B. Lactoperoxidase and ... giving this enzyme the unique capability of easily oxidizing chloride and bromide ions to hypochlorite and hypobromite. ... In peroxidase reactions, the porphyrin molecule also serves as an electron source, being able to delocalize radical electrons ... Heme m contains the two ester bonds at the heme 1- and 5-methyl groups also present in heme l of other mammalian peroxidases, ...
Like horseradish peroxidase, lanthanum is used as an electron-dense tracer in molecular biology. Lanthanum-modified bentonite ( ... Lanthanum metal is obtained from its oxide by heating it with ammonium chloride or fluoride and hydrofluoric acid at 300-400 °C ... Cerium-doped lanthanum bromide and lanthanum chloride are the recent inorganic scintillators, which have a combination of high ... Various compounds of lanthanum and other rare-earth elements (oxides, chlorides, triflates, etc.) are components of various ...
Bahadur also reported having detected ATPase-like and peroxidase-like activity. Bahadur stated that by using molybdenum as a ... Inorganic substances such as colloidal ferric chloride or molybdenum compounds supposedly acted as cofactors and catalysts. ... colloidal molybdenum oxide or potassium nitrate and ferric chloride under sunlight. It appears that this experimental approach ...
Another enzyme, peroxidase, catalyzes a chromogenic reaction (Trinder reaction) of phenol with 4-aminoantipyrine to a purple ... It is also on the list in combination with sodium chloride. The name glucose is derived from Ancient Greek γλεῦκος (gleûkos, " ... Glucose forms a black mass with stannous chloride. In an ammoniacal silver solution, glucose (as well as lactose and dextrin) ...
In research, this reaction is used to stain cells that were prepared with hydrogen peroxidase enzyme, following common ... chloride instead of iron powder or with sodium dithionite in methanol. In its main application, DAB is the precursor to ... One other method uses complexes of injected biocytin with avidin or streptavidin, biotin, and then peroxidase. Hans Schwenecke ... which is conjugated with a peroxidase enzyme. This will bind DAB as a substrate and oxidize it, producing an easily observable ...
Second, the horseradish peroxidase utilizes the hydrogen peroxide to oxidize ABTS to its radical cationic form, ABTS+•. As the ... Another formula consists of indigo carmine , ascorbic acid (Vitamin C), sodium bicarbonate, sodium chloride, copper(II) sulfate ... The experiment is performed in a clear glass vial containing two common enzymes (glucose oxidase and horseradish peroxidase), ...
This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl+, which replaces a ... "New and classic families of secreted fungal heme peroxidases". Appl Microbiol Biotechnol. 87 (3): 871-897. doi:10.1007/s00253- ... Thomas, E. L. (1979). "Myeloperoxidase, hydrogen peroxide, chloride antimicrobial system: Nitrogen-chlorine derivatives of ... hypochlorite degrades to a mixture of chloride, oxygen, and chlorates: 2 ClO− → 2 Cl− + O 2 3 ClO− → 2 Cl− + ClO− 3 This ...
It acts as a mimic of glutathione peroxidase and can also react with peroxynitrite. It is being investigated as a possible ... benzoyl chloride (Route I), by ortho-lithiation of benzanilides followed by oxidative cyclization (Route II) mediated by cupric ... "Ebselen treatment reduces noise induced hearing loss via the mimicry and induction of glutathione peroxidase". Hearing Research ...
Most iodide salts are soluble in water, but often less so than the related chlorides and bromides. Iodide, being large, is less ... peroxidase + H2O2 + tyrosine, histidine, lipid, etc. → iodo-compounds + H2O + 2 e− (antioxidants). Iodargyrite-natural, ... One consequence of this is that sodium iodide is highly soluble in acetone, whereas sodium chloride is not. The low solubility ... For comparison, the lighter halides are considerably smaller: bromide (196 pm), chloride (181 pm), and fluoride (133 pm). In ...
... dimethylarsenic chloride. Some were employed as chemical warfare agents, especially in World War I. This threat led to many ... that take place which may increase the toxicity of arsenic due to MMeAsIII being a potent inhibitor of glutathione peroxidase, ...
Chlorine as chloride ions; very common electrolyte; see sodium, below. Magnesium, required for processing ATP and related ... Molybdenum required for xanthine oxidase and related oxidases Selenium required for peroxidase (antioxidant proteins) Zinc ... typically as sodium chloride (salt). Excessive sodium consumption can deplete calcium and magnesium. Sodium has a role in the ...
Chloride peroxidase (EC 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 ...
Haas R, Tsivunchyk O, Steinbach K. Conversion of adamsite (phenarsarzin chloride) by fungal manganese peroxidase. Appl ... Haas R, Tsivunchyk O, Steinbach K, von Löw E, Scheibner K, Hofrichter M. Conversion of adamsite (phenarsarzin chloride) by ... fungal manganese peroxidase. Appl Microbiol Biotechnol. 2004 Feb. 63(5):564-6. [QxMD MEDLINE Link]. ...
Chloride Peroxidase - Preferred Concept UI. M0004141. Scope note. An enzyme that catalyzes the chlorination of a range of ... An enzyme that catalyzes the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. EC ...
... conjugated to inactivated peroxidase (Sigma, L0390) was added to 33 ml of the gold chloride solution. After a vigorous stirring ... Briefly, 50 ml of 0.01% gold chloride (Sigma) in distilled water was brought to a boil. Then 2 ml of 1% sodium citrate aqueous ... After more rinses in 0.1 m TBS the sections were incubated for 2 hr in avidin-biotin-horseradish peroxidase complex (1:500; ... H2O2 for 1 hr to suppress endogenous peroxidase activity, and then they were rinsed in 0.1m PB and 0.1 m TRIS-buffered saline ( ...
Haas R, Tsivunchyk O, Steinbach K. Conversion of adamsite (phenarsarzin chloride) by fungal manganese peroxidase. Appl ... Haas R, Tsivunchyk O, Steinbach K, von Löw E, Scheibner K, Hofrichter M. Conversion of adamsite (phenarsarzin chloride) by ... fungal manganese peroxidase. Appl Microbiol Biotechnol. 2004 Feb. 63(5):564-6. [QxMD MEDLINE Link]. ...
Get a clear picture of your blood sugar control with the Hemoglobin A1C test. Trust our accurate and convenient test to monitor your diabetes management.. ...
Endogenous peroxidase activity was also blocked. A peroxidase-labeled avidin-biotin complex (Vectastain Elite ABC, Vector ... Final detection was achieved with a solution of diaminobenzidine intensified with nickel chloride (DAB-Ni, Zymed) to give black ... Laboratories, Burlingame, CA, USA) and a solution of diaminobenzidine intensified with nickel chloride (DAB-Ni, Zymed, ...
2 Fragment Peroxidase Conjugated - 008-0304. Versatile and reliable for various research needs. ... 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2 Preservative:. 0.01% (w/v) Gentamicin Sulfate. Do NOT add Sodium ... Specifications for Horse IgG F(ab)2 Peroxidase. Product Details. Description:. Horse IgG F(ab)2 Fragment Peroxidase ... Related products to: Horse IgG F(ab)2 Peroxidase. Horse IgG Fab Fluorescein 008-0205 ...
Efficient labelling of antibodies with horseradish peroxidase using cyanuric chloride. Abuknesha, Ramadan A; Luk, Connie Y; ... An efficient and mild method for labelling of immunoglobulin G (IgG) with horseradish peroxidase (HRP) using cyanuric chloride ... The enzyme was treated first with cyanuric chloride to introduce dichloro triazine and after removal of excess reagent, the ... Ensaio de Imunoadsorção Enzimática , Peroxidase do Rábano Silvestre/química , Imunoglobulina G/química , Triazinas/química , ...
obtained when glycerol 100 mM, ammonium sulfate 0.3%, yeast extract 1.5 g/L, sodium chloride 10 g/L and valine 2 mM were used ... Peroxidases Signaling. Organic compounds are molecules that contain carbon bonded to another element such as hydrogen.. Search ...
After a 20 to 44 hour incubation period in less than 0.05 millimoles of the chlorides of Cd(2+), Zn(2+) and Hg(2+), there was ... no increase of malonaldehyde (542789) or in the activity of glutathione peroxidase and glutathione reductase. There was no ...
2016) Dye decolorizing peroxidases - a new heme-peroxidase family with ancient roots Autoren: Pfanzagl, V; Schaffner, I; ... 2014) Chlorite to chloride and O2 conversion: new lessons from structural and mechanistic investigations of chlorite dismutase ... 2016) Dye-decolorizing peroxidases - a new heme-peroxidase family with ancient roots. Autoren: Pfanzagl, V., Furtmüller, P. G ... Looking for peroxidase substrates and binding site(s) in bifunctional catalase-peroxidase. Autoren: Vlasits, J., Zamocky, M., ...
... in ethylammonium chloride (EAC)/urea DES. The FTIR spectrum of COCytc shows a significant spectral shift upon addition of the ... Two-dimensional infrared spectroscopic study of cytochrome c peroxidase activity in deep eutectic solvent. Structural Dynamics ... Two-dimensional infrared spectroscopic study of cytochrome c peroxidase activity in deep eutectic solvent. In: Structural ... Dive into the research topics of Two-dimensional infrared spectroscopic study of cytochrome c peroxidase activity in deep ...
This product is then neutralized by catalase or glutathione peroxidase.. In the presence of Myeloperoxidase which is a ... lysosomal enzyme, Hydrogen peroxide plus chloride ions are converted to hypochlorous acid. ...
Myeloperoxidase (MPO) is a member of the mammalian heme peroxidase (MHP) multigene family. Whereas all MHPs oxidize specific ... halides to generate the corresponding hypohalous acid, MPO is unique in its capacity to oxidize chloride at physiologic pH to ...
In contrast, eosinophils, which possess eosinophil peroxidase, demonstrated peroxidase staining [30]. .. Animals were housed ... which oxidizes chloride by a single 2-electron transfer to produce the hypochlorous acid (HOCl). Both oxidants - reactive MPO ... Reactive intermediates can be also generated by other heme-peroxidases such as eosinophil peroxidase, lactoperoxidase, thyroid ... Peroxidases.. Chem Biol Interact. 129. 113. 139. 11154738. 26. Scott. CD. Povitsky. A. Dateo. C. Gokcen. T. Willis. PA. 2003. ...
Biotinylated anti-human IgG labeled with strepavidin-peroxidase is used to detect the patients antibody. After rinsing off the ... suspension containing choline chloride to eliminate the need to heat-inactivate serum, ethylene-diamine-tetra-acetic acid (EDTA ...
In brief, gel running buffer was composed of Tris-Base, glycine, Sodium chloride (NaCl), potassium chloride (KCl) purchased ... protein ladders and peroxidase conjugated secondary antibodies anti-rabbit and anti-mouse were purchased from Bio-Rad Inc (USA ...
Then, the NADH reacts with 2-p-iodophenyl-3-p-nitrophenyl-5-phenyltetrazolium chloride (INT) in the presence of diaphorase to ... Hydrogen peroxide, together with peroxidase, permits the oxidative condensation of 3-methyl-N-ethyl-N-β-hydroxy ethyl-O-aniline ... followed by addition of 50 μL of horseradish peroxidase (HRP)-avidin. Samples were incubated for 30 min at 37 °C. Then, they ...
The method employs the reduction of any nitrate to nitrite by vanadium chloride followed by detection of total nitrite by ... and retaining the activity of glutathione peroxidase (GPx) and superoxide dismutase (SOD) in liver [33]. Likewise, the ... The membranes were then probed with horseradish peroxidase conjugated secondary antibodies. Immunoreactive bands were ...
Immunohistochemistry. Sections obtained as described above were treated with 3% H2O2 to block endogenous peroxidase and then ... 5-triphenyltetrazolium chloride (TTC; Sigma Chemical Co.) solution to determine the infarct area, weighed, and photographed ... One unit of MPO activity was defined as that hydrolyzing 1 mmol of peroxidase per minute at 25°C. ... followed by incubation for 1 hour with peroxidase-conjugated anti-mouse secondary Ab (1:2000 dilution; DAKO), and then for 30 ...
Thyroid Peroxidase Antibodies (TPO). WHAT DOES THE THYROID GLAND DO?. The thyroid gland is responsible for regulating how your ... Chloride (Cl). *Carbon Dioxide (CO2). *Calcium (Ca). Kidney Function:. *Blood Urea Nitrogen (BUN) ...
... glutathione peroxidase (GSH-PX), glucagon-like peptide 1 (GLP-1), and LPS-binding protein (LBP) were measured using ELISA kits ... sodium chloride (PubChem CID: 5234), water (PubChem CID: 962), citric acid (PubChem CID: 311), butyric acid (PubChem CID: 264 ...
sodium chloride, or common salt. [edit] Trace minerals. Many elements are required in smaller amounts (microgram quantities), ... peroxidase (antioxidant proteins). *Zinc required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, ... chloride ions; very common electrolyte; see sodium, below. *ATP and related reactions (builds bone, causes strong peristalsis, ... Dietary Reference Intakes: Water, Potassium, Sodium, Chloride, and Sulfate, Food and Nutrition Board ...
3 General references Selenium (Se) is a part of the enzyme glutathione peroxidase, which metabolizes hydroperoxides formed from ... Four cations: Sodium, potassium, calcium, and magnesium Two accompanying anions: Chloride and phosphorus Daily requirements ... Diagnosis of selenium deficiency is made clinically or sometimes by measuring glutathione peroxidase activity or plasma ... Selenium (Se) is a part of the enzyme glutathione peroxidase, which metabolizes hydroperoxides formed from polyunsaturated ...
Lefebvre E., Legube B. Coagulation-flocculation by ferric chloride of some organic compounds in aqueous solution. Water Res. ... Wu J., Rudy K., Spark J. Oxidation of aqueous phenol by ozone or peroxidase. Adv. Environ. Res. 2000. 4(4): 339. https://doi. ...
Endogenous peroxidase was blocked with 0.3% hydrogen peroxide in phosphate buffered saline (PBS) for 30 minutes and endogenous ... Staining reaction was performed overnight with 4-Nitro blue tetrazolium chloride (NBT) (Roche) and X-phosphate/5-Bromo-4-chloro ...
  • The catalytic acid base, required to cleave the peroxide O-O bond, is glutamic acid rather than histidine as in horseradish peroxidase. (
  • The heme-containing chloroperoxidase (CPO) exhibits peroxidase, catalase and cytochrome P450-like activities in addition to catalyzing halogenation reactions. (
  • Anti-oxidative enzymes of plants include glutathione peroxidase (GPX), superoxide dismutase (SOD), ascorbate peroxidase (APX), glutathione S-transferase (GST), dehydroascorbate reductase (DHAR), glutathione reductase (GR), peroxide reduction (PRX), mono-hydro ascorbate reductase (MDAR), and catalase (CAT). (
  • CCl 4 injection produced a significant rise in serum markers of oxidative stress and lipid peroxidation product malondialdehyde along with the reduction of antioxidant enzymes such as superoxide dismuta, catalase and glutathion peroxidase. (
  • Chloride peroxidase (EC is a family of enzymes that catalyzes the chlorination of organic compounds. (
  • Assay by immunoelectrophoresis resulted in a single precipitin arc against anti-Peroxidase, anti-Horse IgG, anti-Horse IgG F(ab')2 and anti-Horse Serum. (
  • The antigen is prepared from a modified Venereal Disease Research Laboratory (VDRL) antigen suspension containing choline chloride to eliminate the need to heat-inactivate serum, ethylene-diamine-tetra-acetic acid (EDTA) to enhance the stability of the suspension, and finely divided charcoal particles as a visualizing agent. (
  • More than 50% of these patients have high serum antithyroid peroxidase antibody levels, and nearly 50% have overt hypothyroidism. (
  • After a 20 to 44 hour incubation period in less than 0.05 millimoles of the chlorides of Cd(2+), Zn(2+) and Hg(2+), there was no increase of malonaldehyde (542789) or in the activity of glutathione peroxidase and glutathione reductase. (
  • Saliva contains a number of components, including various electrolytes, glycoproteins, enzymes, and mucus, as well as secretory immunoglobulin A, lactoferrin, lysozyme, and peroxidase-with the latter 4 components important in that they exhibit antibacterial activity. (
  • Biotinylated anti-human IgG labeled with strepavidin-peroxidase is used to detect the patient's antibody. (
  • The systematic name of this enzyme class is chloride:hydrogen-peroxide oxidoreductase. (
  • Here, to elucidate the effects of DESs on the peroxidase activity of cytochrome c, we carried out linear and nonlinear infrared spectroscopic studies of the CO stretch mode of carbon monoxide cytochrome c (COCytc) in ethylammonium chloride (EAC)/urea DES. (
  • The experimental results lead us to propose a hypothesis that the DES increases the population of the conformer with distal ligand lysines close to the reaction center through the combining effect of urea and EAC, which results in the enhancement of the peroxidase activity of cytochrome c. (
  • This enzyme combines the inorganic substrates chloride and hydrogen peroxide to produce the equivalent of Cl+, which replaces a proton in hydrocarbon substrate: R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O In fact the source of "Cl+" is hypochlorous acid (HOCl). (
  • This enzyme belongs to the family of oxidoreductases, specifically those acting on a peroxide as acceptors (peroxidases). (
  • An enzyme that catalyzes the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. (
  • Selenium (Se) is a part of the enzyme glutathione peroxidase, which metabolizes hydroperoxides formed from polyunsaturated fatty acids. (
  • Diagnosis of selenium deficiency is made clinically or sometimes by measuring glutathione peroxidase activity or plasma selenium , but neither of these tests is readily available. (
  • Selenium is an essential cofactor of glutathione peroxidase, a potent antioxidant. (
  • Four cations: Sodium, potassium, calcium, and magnesium Two accompanying anions: Chloride and phosphorus Daily requirements range from. (
  • Potassium (as potassium chloride). (
  • 2,3,7,8-Tetrachlorodibenzo- p -dioxin as an antiestrogen: Effect on rat uterine peroxidase activity. (
  • Horse IgG F(ab')2 Peroxidase can be utilized as a control or standard reagent in Western Blotting and ELISA experiments. (
  • The amount of glutathione and the glutathione peroxidase activity in kidney decreased with increasing doses of mercuric chloride. (
  • The reduced glutathione peroxidase activity was due to a reduction in selenium-dependent glutathione peroxidase activity. (
  • Diagnosis of selenium deficiency is made clinically or sometimes by measuring glutathione peroxidase activity or plasma selenium , but neither of these tests is readily available. (
  • 11. Selenium supplementation on plasma glutathione peroxidase activity in patients with end-stage chronic renal failure. (
  • 15. Reduced platelet glutathione peroxidase activity and serum selenium concentration in atopic asthmatic patients. (
  • TSH, free T3 and T4 are taken, along with antithyroid-peroxidase and antithyroglobulin antibodies. (
  • Both Hannah and Quentin have high levels of TSH and low T3 and T4 levels, but Hannah has positive antithyroid-peroxidase and antithyroglobulin antibodies. (
  • Is prepared by treating (s) + )-propylenediaminc id raacetic tetraamide with sodium chloride 4g wool fat or ointment with 0.4 % [38] ions at a better feel for the pessaries, it is protein bound, the first dependent homocystemne methyl transferase reaction and analyzing pharmacostatistical drug interaction reference when combining with an hlb of a high-fat meal. (
  • Four cations: Sodium, potassium, calcium, and magnesium Two accompanying anions: Chloride and phosphorus Daily requirements range from. (
  • The upland cotton genotypes FMT 701 and Fibermax 966 have distinct morphophysiological characteristics due to their different genetic constitution, and thus, it is possible to have differences in the activity of the antioxidant complex enzymes (superoxide dismutase, catalase and peroxidase) as well as the main parameters photosynthesis and leaf anatomical, depending on the application of increasing doses of growth regulator, mepiquat chloride (MC). (
  • or enzymes capable or depositing insoluble reaction products, e.g. peroxidase or alkaline phosphatase, the presence, location, or quantity of a biotin probe can be established. (
  • The present study was planned to evaluate the effectiveness of Withania somnifera against aluminium chloride-induced testicular toxicity and impaired fertility. (
  • These findings thus revealed the ameliorating potential of Withania somnifera against aluminium chloride-induced testicular toxicity and impaired fertility. (
  • Therefore, this study investigated Zingiber officinale (ZO) neuroprotective potential against aluminium chloride (AlCl 3 )-induced neurotoxicity in Swiss mice. (
  • Therefore, this study aimed to investigate Zingiber officinale ethanol extract and its fractions (dichloromethane and n-hexane) in aluminium chloride-induced neurotoxicity on Swiss mice. (
  • The biotinylated peptide is able to interact with streptavidin-horseradish peroxidase (SA-HRP), which catalyzes the substrate solution composed of 3,3',5,5'-tetramethylbenzidine (TMB) and hydrogen peroxidase to produce a blue solution. (
  • The enzyme-substrate reaction is stopped by hydrogen chloride (HCI) and the solution turns yellow. (
  • Hydrogen peroxide is used to quench endogenous peroxidase in immunohistochemical staining. (
  • The level of lipid peroxidation was not changed by increasing doses of mercuric chloride, and hence was not a primary toxic mechanism in acute nephrotoxicity induced by mercuric chloride. (
  • No experimento de campo, a enzima peroxidase (POD) aumentou sua atividade em função das doses de CM nos genótipos, desintoxicando as células dos radicais livres formados, e em casa de vegetação o CM não alterou a atividade das enzimas antioxidantes, sugerindo ausência de estresse oxidativo nos dois experimentos. (
  • Previous studies have demonstrated an inverse relationship between dose size and relative whole-body retention of mercury after oral administration of mercuric chloride to mice. (
  • An enzyme that catalyzes the chlorination of a range of organic molecules, forming stable carbon-chloride bonds. (