A mixed function oxidase enzyme which during hemoglobin catabolism catalyzes the degradation of heme to ferrous iron, carbon monoxide and biliverdin in the presence of molecular oxygen and reduced NADPH. The enzyme is induced by metals, particularly cobalt. EC 1.14.99.3.
The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins.
A ubiquitous stress-responsive enzyme that catalyzes the oxidative cleavage of HEME to yield IRON; CARBON MONOXIDE; and BILIVERDIN.
1,3,6,7-Tetramethyl-4,5-dicarboxyethyl-2,8-divinylbilenone. Biosynthesized from hemoglobin as a precursor of bilirubin. Occurs in the bile of AMPHIBIANS and of birds, but not in normal human bile or serum.
Porphyrins with four methyl, two vinyl, and two propionic acid side chains attached to the pyrrole rings. Protoporphyrin IX occurs in hemoglobin, myoglobin, and most of the cytochromes.
Carbon monoxide (CO). A poisonous colorless, odorless, tasteless gas. It combines with hemoglobin to form carboxyhemoglobin, which has no oxygen carrying capacity. The resultant oxygen deprivation causes headache, dizziness, decreased pulse and respiratory rates, unconsciousness, and death. (From Merck Index, 11th ed)
Porphyrins which are combined with a metal ion. The metal is bound equally to all four nitrogen atoms of the pyrrole rings. They possess characteristic absorption spectra which can be utilized for identification or quantitative estimation of porphyrins and porphyrin-bound compounds.
Chloro(7,12-diethenyl-3,8,13,17-tetramethyl-21H,23H-porphine-2,18-dipropanoato(4-)-N(21),N(22),N(23),N(24)) ferrate(2-) dihydrogen.
Porphyrins with four methyl and two propionic acid side chains attached to the pyrrole rings.
Widely distributed enzymes that carry out oxidation-reduction reactions in which one atom of the oxygen molecule is incorporated into the organic substrate; the other oxygen atom is reduced and combined with hydrogen ions to form water. They are also known as monooxygenases or hydroxylases. These reactions require two substrates as reductants for each of the two oxygen atoms. There are different classes of monooxygenases depending on the type of hydrogen-providing cosubstrate (COENZYMES) required in the mixed-function oxidation.
Porphyrins with four methyl, two ethyl, and two propionic acid side chains attached to the pyrrole rings.
Oxidases that specifically introduce DIOXYGEN-derived oxygen atoms into a variety of organic molecules.
An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis.
A non-heme IRON enzyme that catalyzes the conversion of MYOINOSITOL to D-glucuronic acid. The reaction is the first committed step in MYOINOSITOL catabolic pathway. This enzyme was formerly characterized as EC 1.13.1.11 and 1.99.2.6.
A carboxy-lyase that plays a key role in photosynthetic carbon assimilation in the CALVIN-BENSON CYCLE by catalyzing the formation of 3-phosphoglycerate from ribulose 1,5-biphosphate and CARBON DIOXIDE. It can also utilize OXYGEN as a substrate to catalyze the synthesis of 2-phosphoglycolate and 3-phosphoglycerate in a process referred to as photorespiration.
A hypnotic and sedative. Its use has been largely superseded by other drugs.
A group of compounds containing the porphin structure, four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. The nature of the side chain is indicated by a prefix, as uroporphyrin, hematoporphyrin, etc. The porphyrins, in combination with iron, form the heme component in biologically significant compounds such as hemoglobin and myoglobin.
A bile pigment that is a degradation product of HEME.
An enzyme of the transferase class that catalyzes condensation of the succinyl group from succinyl coenzyme A with glycine to form delta-aminolevulinate. It is a pyridoxyal phosphate protein and the reaction occurs in mitochondria as the first step of the heme biosynthetic pathway. The enzyme is a key regulatory enzyme in heme biosynthesis. In liver feedback is inhibited by heme. EC 2.3.1.37.
A trace element that is a component of vitamin B12. It has the atomic symbol Co, atomic number 27, and atomic weight 58.93. It is used in nuclear weapons, alloys, and pigments. Deficiency in animals leads to anemia; its excess in humans can lead to erythrocytosis.
Proteins that contain an iron-porphyrin, or heme, prosthetic group resembling that of hemoglobin. (From Lehninger, Principles of Biochemistry, 1982, p480)
A dioxygenase with specificity for the oxidation of the indoleamine ring of TRYPTOPHAN. It is a LIVER-specific enzyme that is the first and rate limiting enzyme in the kynurenine pathway of TRYPTOPHAN catabolism.
A flavoprotein that catalyzes the reduction of heme-thiolate-dependent monooxygenases and is part of the microsomal hydroxylating system. EC 1.6.2.4.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
Four PYRROLES joined by one-carbon units linking position 2 of one to position 5 of the next. The conjugated bond system results in PIGMENTATION.
Inorganic compounds that contain tin as an integral part of the molecule.
Open chain tetrapyrroles that function as light harvesting chromophores in PHYCOBILIPROTEINS.
A drug-metabolizing enzyme of the hepatic microsomal oxidase system which catalyzes the oxidation of the N-methyl group of ethylmorphine with the formation of formaldehyde.
A trace element that is required in bone formation. It has the atomic symbol Sn, atomic number 50, and atomic weight 118.71.
A species of gram-positive, asporogenous bacteria in which three cultural types are recognized. These types (gravis, intermedius, and mitis) were originally given in accordance with the clinical severity of the cases from which the different strains were most frequently isolated. This species is the causative agent of DIPHTHERIA.
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).
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A condition characterized by an abnormal increase of BILIRUBIN in the blood, which may result in JAUNDICE. Bilirubin, a breakdown product of HEME, is normally excreted in the BILE or further catabolized before excretion in the urine.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
The presence of free HEMOGLOBIN in the URINE, indicating hemolysis of ERYTHROCYTES within the vascular system. After saturating the hemoglobin-binding proteins (HAPTOGLOBINS), free hemoglobin begins to appear in the urine.
Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.
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).
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
Hemopexin is a plasma glycoprotein that binds heme with high affinity, preventing its toxic effects and facilitating its clearance, thus playing a crucial role in iron metabolism and protection against oxidative stress.
The metal-free blue phycobilin pigment in a conjugated chromoprotein of blue-green algae. It functions as light-absorbing substance together with chlorophylls.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
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.
Plants of the division Rhodophyta, commonly known as red algae, in which the red pigment (PHYCOERYTHRIN) predominates. However, if this pigment is destroyed, the algae can appear purple, brown, green, or yellow. Two important substances found in the cell walls of red algae are AGAR and CARRAGEENAN. Some rhodophyta are notable SEAWEED (macroalgae).
Inorganic compounds that contain sodium as an integral part of the molecule.
A mitochondrial enzyme found in a wide variety of cells and tissues. It is the final enzyme in the 8-enzyme biosynthetic pathway of HEME. Ferrochelatase catalyzes ferrous insertion into protoporphyrin IX to form protoheme or heme. Deficiency in this enzyme results in ERYTHROPOIETIC PROTOPORPHYRIA.
A basic-leucine zipper transcription factor that was originally described as a transcriptional regulator controlling expression of the BETA-GLOBIN gene. It may regulate the expression of a wide variety of genes that play a role in protecting cells from oxidative damage.
An allylic compound that acts as a suicide inactivator of CYTOCHROME P450 by covalently binding to its heme moiety or surrounding protein.
An enzyme that catalyzes the formation of porphobilinogen from two molecules of 5-aminolevulinic acid. EC 4.2.1.24.
A superfamily of hundreds of closely related HEMEPROTEINS found throughout the phylogenetic spectrum, from animals, plants, fungi, to bacteria. They include numerous complex monooxygenases (MIXED FUNCTION OXYGENASES). In animals, these P-450 enzymes serve two major functions: (1) biosynthesis of steroids, fatty acids, and bile acids; (2) metabolism of endogenous and a wide variety of exogenous substrates, such as toxins and drugs (BIOTRANSFORMATION). They are classified, according to their sequence similarities rather than functions, into CYP gene families (>40% homology) and subfamilies (>59% homology). For example, enzymes from the CYP1, CYP2, and CYP3 gene families are responsible for most drug metabolism.
A compound produced from succinyl-CoA and GLYCINE as an intermediate in heme synthesis. It is used as a PHOTOCHEMOTHERAPY for actinic KERATOSIS.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The rate dynamics in chemical or physical systems.
Analysis of the intensity of Raman scattering of monochromatic light as a function of frequency of the scattered light.
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.
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
The oxygen-carrying proteins of ERYTHROCYTES. They are found in all vertebrates and some invertebrates. The number of globin subunits in the hemoglobin quaternary structure differs between species. Structures range from monomeric to a variety of multimeric arrangements.
Inorganic salts or organic esters of arsenious acid.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
A free radical gas produced endogenously by a variety of mammalian cells, synthesized from ARGININE by NITRIC OXIDE SYNTHASE. Nitric oxide is one of the ENDOTHELIUM-DEPENDENT RELAXING FACTORS released by the vascular endothelium and mediates VASODILATION. It also inhibits platelet aggregation, induces disaggregation of aggregated platelets, and inhibits platelet adhesion to the vascular endothelium. Nitric oxide activates cytosolic GUANYLATE CYCLASE and thus elevates intracellular levels of CYCLIC GMP.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Ribulose substituted by one or more phosphoric acid moieties.
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.
Non-heme iron-containing enzymes that incorporate two atoms of OXYGEN into the substrate. They are important in biosynthesis of FLAVONOIDS; GIBBERELLINS; and HYOSCYAMINE; and for degradation of AROMATIC HYDROCARBONS.
A 1:1 molar complex of heme or hematin and albumin formed after the dissociation of methemoglobin into heme or hematin and globin in plasma. This complex, which imparts a coffee-brown color to plasma, occurs in hemolytic and hemorrhagic disorders. Its presence in plasma is used as a test to differentiate between hemorrhagic and edematous pancreatitis.
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.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
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.
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)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types.
An NADPH-dependent enzyme that catalyzes the conversion of L-ARGININE and OXYGEN to produce CITRULLINE and NITRIC OXIDE.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Proteins found in any species of bacterium.
Body organ that filters blood for the secretion of URINE and that regulates ion concentrations.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Physical changes in the growth patterns of a plant brought on by sustained absence of light. These changes are characterized by lengthened internodes which produce long weak stems, fewer leaves, and pale yellow color (chlorosis). The physiological basis for etiolation is induction of the phytohormone, AUXIN.
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.
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.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A blue-green biliprotein widely distributed in the plant kingdom.

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.

Heme Oxygenase-1 (HO-1) is an inducible enzyme that catalyzes the degradation of heme into biliverdin, iron, and carbon monoxide. It is a rate-limiting enzyme in the oxidative degradation of heme. HO-1 is known to play a crucial role in cellular defense against oxidative stress and inflammation. It is primarily located in the microsomes of many tissues, including the spleen, liver, and brain. Induction of HO-1 has been shown to have cytoprotective effects, while deficiency in HO-1 has been associated with several pathological conditions, such as vascular diseases, neurodegenerative disorders, and cancer.

Biliverdine is a greenish pigment that is a byproduct of the breakdown of heme, which is a component of hemoglobin in red blood cells. It is formed when bilirubin, another byproduct of heme degradation, is reduced in the liver. Biliverdine is then converted back to bilirubin and excreted from the body as part of bile.

Elevated levels of biliverdine in the blood can indicate liver dysfunction or other medical conditions that affect the breakdown of heme. It may also be present in high concentrations in certain types of hemolytic anemia, where there is excessive destruction of red blood cells and subsequent release of large amounts of heme into the circulation.

Protoporphyrins are organic compounds that are the immediate precursors to heme in the porphyrin synthesis pathway. They are composed of a porphyrin ring, which is a large, complex ring made up of four pyrrole rings joined together, with an acetate and a propionate side chain at each pyrrole. Protoporphyrins are commonly found in nature and are important components of many biological systems, including hemoglobin, the protein in red blood cells that carries oxygen throughout the body.

There are several different types of protoporphyrins, including protoporphyrin IX, which is the most common form found in humans and other animals. Protoporphyrins can be measured in the blood or other tissues as a way to diagnose or monitor certain medical conditions, such as lead poisoning or porphyrias, which are rare genetic disorders that affect the production of heme. Elevated levels of protoporphyrins in the blood or tissues can indicate the presence of these conditions and may require further evaluation and treatment.

Carbon monoxide (CO) is a colorless, odorless, and tasteless gas that is slightly less dense than air. It is toxic to hemoglobic animals when encountered in concentrations above about 35 ppm. This compound is a product of incomplete combustion of organic matter, and is a major component of automobile exhaust.

Carbon monoxide is poisonous because it binds to hemoglobin in red blood cells much more strongly than oxygen does, forming carboxyhemoglobin. This prevents the transport of oxygen throughout the body, which can lead to suffocation and death. Symptoms of carbon monoxide poisoning include headache, dizziness, weakness, nausea, vomiting, confusion, and disorientation. Prolonged exposure can lead to unconsciousness and death.

Carbon monoxide detectors are commonly used in homes and other buildings to alert occupants to the presence of this dangerous gas. It is important to ensure that these devices are functioning properly and that they are placed in appropriate locations throughout the building. Additionally, it is essential to maintain appliances and heating systems to prevent the release of carbon monoxide into living spaces.

Metalloporphyrins are a type of porphyrin molecule that contain a metal ion at their center. Porphyrins are complex organic compounds containing four modified pyrrole rings connected to form a planar, aromatic ring known as a porphine. When a metal ion is incorporated into the center of the porphyrin ring, it forms a metalloporphyrin.

These molecules have great biological significance, as they are involved in various essential processes within living organisms. For instance, heme, a type of iron-containing porphyrin, plays a crucial role in oxygen transport and storage in the body by forming part of hemoglobin and myoglobin molecules. Chlorophyll, another metalloporphyrin with magnesium at its center, is essential for photosynthesis in plants, algae, and some bacteria.

Metalloporphyrins have also found applications in several industrial and medical fields, including catalysis, sensors, and pharmaceuticals. Their unique structure and properties make them valuable tools for researchers and scientists to study and utilize in various ways.

Hemin is defined as the iron(III) complex of protoporphyrin IX, which is a porphyrin derivative. It is a naturally occurring substance that is involved in various biological processes, most notably in the form of heme, which is a component of hemoglobin and other hemoproteins. Hemin is also used in medical research and therapy, such as in the treatment of methemoglobinemia and lead poisoning.

Deuteroporphyrins are porphyrin derivatives that contain two carboxylic acid side chains. They are intermediates in the biosynthesis of heme and chlorophyll, which are essential molecules for biological processes such as oxygen transport and photosynthesis, respectively.

Deuteroporphyrins can be further classified into isomers based on the position of the carboxylic acid side chains. The most common isomer is deuteroporphyrin IX, which has the carboxylic acid side chains located at positions 1 and 2 relative to the pyrrole nitrogen atoms.

Deuteroporphyrins have been studied in various medical contexts, including as potential markers of porphyria, a group of metabolic disorders characterized by the accumulation of porphyrin precursors. Additionally, deuteroporphyrins and their derivatives have been investigated for their potential use in photodynamic therapy, a treatment modality that uses light-activated drugs to destroy cancer cells.

Mixed Function Oxygenases (MFOs) are a type of enzyme that catalyze the addition of one atom each from molecular oxygen (O2) to a substrate, while reducing the other oxygen atom to water. These enzymes play a crucial role in the metabolism of various endogenous and exogenous compounds, including drugs, carcinogens, and environmental pollutants.

MFOs are primarily located in the endoplasmic reticulum of cells and consist of two subunits: a flavoprotein component that contains FAD or FMN as a cofactor, and an iron-containing heme protein. The most well-known example of MFO is cytochrome P450, which is involved in the oxidation of xenobiotics and endogenous compounds such as steroids, fatty acids, and vitamins.

MFOs can catalyze a variety of reactions, including hydroxylation, epoxidation, dealkylation, and deamination, among others. These reactions often lead to the activation or detoxification of xenobiotics, making MFOs an important component of the body's defense system against foreign substances. However, in some cases, these reactions can also produce reactive intermediates that may cause toxicity or contribute to the development of diseases such as cancer.

Mesoporphyrins are a type of porphyrin, which are organic compounds containing four pyrrole rings connected by methine bridges in a cyclic arrangement. Porphyrins are important components of various biological molecules such as hemoglobin, myoglobin, and cytochromes.

Mesoporphyrins have a specific structure with two propionic acid side chains and two acetic acid side chains attached to the pyrrole rings. They are intermediates in the biosynthesis of heme, which is a complex formed by the insertion of iron into protoporphyrin IX, a type of porphyrin.

Mesoporphyrins have been used in medical research and clinical settings as photosensitizers for photodynamic therapy (PDT), a treatment that uses light to activate a photosensitizing agent to destroy abnormal cells or tissues. In particular, mesoporphyrin IX has been used for the PDT treatment of various types of cancer, such as bladder, esophageal, and lung cancer, as well as for the treatment of age-related macular degeneration (AMD), a leading cause of vision loss in older adults.

It is important to note that mesoporphyrins are not typically used as a diagnostic tool or a therapeutic agent in routine clinical practice, but rather as part of experimental research and clinical trials.

Oxygenases are a class of enzymes that catalyze the incorporation of molecular oxygen (O2) into their substrates. They play crucial roles in various biological processes, including the biosynthesis of many natural products, as well as the detoxification and degradation of xenobiotics (foreign substances).

There are two main types of oxygenases: monooxygenases and dioxygenases. Monooxygenases introduce one atom of molecular oxygen into a substrate while reducing the other to water. An example of this type of enzyme is cytochrome P450, which is involved in drug metabolism and steroid hormone synthesis. Dioxygenases, on the other hand, incorporate both atoms of molecular oxygen into their substrates, often leading to the formation of new carbon-carbon bonds or the cleavage of existing ones.

It's important to note that while oxygenases are essential for many life-sustaining processes, they can also contribute to the production of harmful reactive oxygen species (ROS) during normal cellular metabolism. An imbalance in ROS levels can lead to oxidative stress and damage to cells and tissues, which has been linked to various diseases such as cancer, neurodegeneration, and cardiovascular disease.

Enzyme induction is a process by which the activity or expression of an enzyme is increased in response to some stimulus, such as a drug, hormone, or other environmental factor. This can occur through several mechanisms, including increasing the transcription of the enzyme's gene, stabilizing the mRNA that encodes the enzyme, or increasing the translation of the mRNA into protein.

In some cases, enzyme induction can be a beneficial process, such as when it helps the body to metabolize and clear drugs more quickly. However, in other cases, enzyme induction can have negative consequences, such as when it leads to the increased metabolism of important endogenous compounds or the activation of harmful procarcinogens.

Enzyme induction is an important concept in pharmacology and toxicology, as it can affect the efficacy and safety of drugs and other xenobiotics. It is also relevant to the study of drug interactions, as the induction of one enzyme by a drug can lead to altered metabolism and effects of another drug that is metabolized by the same enzyme.

Inositol oxygenase is not a widely recognized medical term, but it does refer to an enzyme that is involved in certain biochemical reactions. Here is a general definition:

Inositol oxygenase (IO) is an enzyme that catalyzes the oxidation of myo-inositol to form D-glucuronic acid and S-d-glucuronosyl-L-serine, using molecular oxygen as a co-substrate. This reaction is part of the inositol metabolic pathway, which plays a role in various cellular processes such as signal transduction, lipid synthesis, and stress response. In humans, mutations in the IO gene have been associated with neurological disorders and developmental abnormalities.

Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is a crucial enzyme in the Calvin cycle, which is a process that plants use to convert carbon dioxide into glucose during photosynthesis. RuBisCO catalyzes the reaction between ribulose-1,5-bisphosphate and carbon dioxide, resulting in the formation of two molecules of 3-phosphoglycerate, which can then be converted into glucose.

RuBisCO is considered to be the most abundant enzyme on Earth, making up as much as 50% of the soluble protein found in leaves. It is a large and complex enzyme, consisting of eight small subunits and eight large subunits that are arranged in a barrel-shaped structure. The active site of the enzyme, where the reaction between ribulose-1,5-bisphosphate and carbon dioxide takes place, is located at the interface between two large subunits.

RuBisCO also has a secondary function as an oxygenase, which can lead to the production of glycolate, a toxic compound for plants. This reaction occurs when the enzyme binds with oxygen instead of carbon dioxide and is more prevalent in environments with low carbon dioxide concentrations and high oxygen concentrations. The glycolate produced during this process needs to be recycled through a series of reactions known as photorespiration, which can result in significant energy loss for the plant.

Glutethimide is a sedative-hypnotic drug that was previously used for the treatment of insomnia and anxiety disorders. It belongs to the class of drugs known as non-barbiturate hypnotics. Glutethimide works by depressing the central nervous system (CNS), producing a calming effect on the brain.

Due to its potential for abuse, addiction, and its narrow therapeutic index, glutethimide is no longer commonly used in clinical practice. It has been replaced by safer and more effective sleep aids with fewer side effects and lower potential for misuse.

It's important to note that the use of glutethimide should be under the strict supervision of a healthcare professional, and it should only be taken as prescribed. Misuse or overuse of this medication can lead to serious health consequences, including respiratory depression, coma, and even death.

Porphyrins are complex organic compounds that contain four pyrrole rings joined together by methine bridges (=CH-). They play a crucial role in the biochemistry of many organisms, as they form the core structure of various heme proteins and other metalloproteins. Some examples of these proteins include hemoglobin, myoglobin, cytochromes, and catalases, which are involved in essential processes such as oxygen transport, electron transfer, and oxidative metabolism.

In the human body, porphyrins are synthesized through a series of enzymatic reactions known as the heme biosynthesis pathway. Disruptions in this pathway can lead to an accumulation of porphyrins or their precursors, resulting in various medical conditions called porphyrias. These disorders can manifest as neurological symptoms, skin lesions, and gastrointestinal issues, depending on the specific type of porphyria and the site of enzyme deficiency.

It is important to note that while porphyrins are essential for life, their accumulation in excessive amounts or at inappropriate locations can result in pathological conditions. Therefore, understanding the regulation and function of porphyrin metabolism is crucial for diagnosing and managing porphyrias and other related disorders.

Bilirubin is a yellowish pigment that is produced by the liver when it breaks down old red blood cells. It is a normal byproduct of hemoglobin metabolism and is usually conjugated (made water-soluble) in the liver before being excreted through the bile into the digestive system. Elevated levels of bilirubin can cause jaundice, a yellowing of the skin and eyes. Increased bilirubin levels may indicate liver disease or other medical conditions such as gallstones or hemolysis. It is also measured to assess liver function and to help diagnose various liver disorders.

5-Aminolevulinate synthase (ALAS) is an enzyme that catalyzes the first step in heme biosynthesis, a metabolic pathway that produces heme, a porphyrin ring with an iron atom at its center. Heme is a crucial component of hemoglobin, cytochromes, and other important molecules in the body.

ALAS exists in two forms: ALAS1 and ALAS2. ALAS1 is expressed in all tissues, while ALAS2 is primarily expressed in erythroid cells (precursors to red blood cells). The reaction catalyzed by ALAS involves the condensation of glycine and succinyl-CoA to form 5-aminolevulinate.

Deficiencies or mutations in the ALAS2 gene can lead to a rare genetic disorder called X-linked sideroblastic anemia, which is characterized by abnormal red blood cell maturation and iron overload in mitochondria.

Cobalt is a chemical element with the symbol Co and atomic number 27. It is a hard, silver-white, lustrous, and brittle metal that is found naturally only in chemically combined form, except for small amounts found in meteorites. Cobalt is used primarily in the production of magnetic, wear-resistant, and high-strength alloys, as well as in the manufacture of batteries, magnets, and pigments.

In a medical context, cobalt is sometimes used in the form of cobalt-60, a radioactive isotope, for cancer treatment through radiation therapy. Cobalt-60 emits gamma rays that can be directed at tumors to destroy cancer cells. Additionally, small amounts of cobalt are present in some vitamin B12 supplements and fortified foods, as cobalt is an essential component of vitamin B12. However, exposure to high levels of cobalt can be harmful and may cause health effects such as allergic reactions, lung damage, heart problems, and neurological issues.

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.

Tryptophan oxygenase, also known as tryptophan 2,3-dioxygenase (TDO) or tryptophan pyrrolase, is an enzyme that catalyzes the breakdown of the essential amino acid tryptophan. This enzyme requires molecular oxygen and plays a crucial role in regulating tryptophan levels within the body.

The reaction catalyzed by tryptophan oxygenase involves the oxidation of the indole ring of tryptophan, leading to the formation of N-formylkynurenine. This metabolite is further broken down through several enzymatic steps to produce other biologically active compounds, such as kynurenine and niacin (vitamin B3).

Tryptophan oxygenase activity is primarily found in the liver and is induced by various factors, including corticosteroids, cytokines, and tryptophan itself. The regulation of this enzyme has implications for several physiological processes, such as immune response, neurotransmitter synthesis, and energy metabolism. Dysregulation of tryptophan oxygenase activity can contribute to the development of various pathological conditions, including neurological disorders and cancer.

NADPH-ferrihemoprotein reductase, also known as diaphorase or NO synthase reductase, is an enzyme that catalyzes the reduction of ferrihemoproteins using NADPH as a reducing cofactor. This reaction plays a crucial role in various biological processes such as the detoxification of certain compounds and the regulation of cellular signaling pathways.

The systematic name for this enzyme is NADPH:ferrihemoprotein oxidoreductase, and it belongs to the family of oxidoreductases that use NADH or NADPH as electron donors. The reaction catalyzed by this enzyme can be represented as follows:

NADPH + H+ + ferrihemoprotein ↔ NADP+ + ferrohemoprotein

In this reaction, the ferric (FeIII) form of hemoproteins is reduced to its ferrous (FeII) form by accepting electrons from NADPH. This enzyme is widely distributed in various tissues and organisms, including bacteria, fungi, plants, and animals. It has been identified as a component of several multi-enzyme complexes involved in different metabolic pathways, such as nitric oxide synthase (NOS) and cytochrome P450 reductase.

In summary, NADPH-ferrihemoprotein reductase is an essential enzyme that catalyzes the reduction of ferrihemoproteins using NADPH as a reducing agent, playing a critical role in various biological processes and metabolic pathways.

In the context of medicine, iron is an essential micromineral and key component of various proteins and enzymes. It plays a crucial role in oxygen transport, DNA synthesis, and energy production within the body. Iron exists in two main forms: heme and non-heme. Heme iron is derived from hemoglobin and myoglobin in animal products, while non-heme iron comes from plant sources and supplements.

The recommended daily allowance (RDA) for iron varies depending on age, sex, and life stage:

* For men aged 19-50 years, the RDA is 8 mg/day
* For women aged 19-50 years, the RDA is 18 mg/day
* During pregnancy, the RDA increases to 27 mg/day
* During lactation, the RDA for breastfeeding mothers is 9 mg/day

Iron deficiency can lead to anemia, characterized by fatigue, weakness, and shortness of breath. Excessive iron intake may result in iron overload, causing damage to organs such as the liver and heart. Balanced iron levels are essential for maintaining optimal health.

Tetrapyrroles are a class of organic compounds that contain four pyrrole rings joined together in a macrocyclic structure. They are important in biology because they form the core structure of many essential cofactors and prosthetic groups in proteins, including heme, chlorophyll, and cobalamin (vitamin B12).

Heme is a tetrapyrrole that contains iron and is a crucial component of hemoglobin, the protein responsible for oxygen transport in red blood cells. Chlorophyll is another tetrapyrrole that contains magnesium and plays a vital role in photosynthesis, the process by which plants convert light energy into chemical energy. Cobalamin contains cobalt and is essential for DNA synthesis, fatty acid metabolism, and neurotransmitter synthesis.

Abnormalities in tetrapyrrole biosynthesis can lead to various diseases, such as porphyrias, which are characterized by the accumulation of toxic intermediates in the heme biosynthetic pathway.

Tin compounds refer to chemical substances that contain tin (Sn) combined with one or more other elements. Tin can form various types of compounds, including oxides, sulfides, halides, and organometallic compounds. These compounds have different properties and uses depending on the other element(s) they are combined with.

For example:

* Tin (IV) oxide (SnO2) is a white powder used as an opacifying agent in glass and ceramics, as well as a component in some types of batteries.
* Tin (II) sulfide (SnS) is a black or brown solid used in the manufacture of some types of semiconductors.
* Tin (IV) chloride (SnCl4) is a colorless liquid used as a catalyst in the production of polyvinyl chloride (PVC) and other plastics.
* Organotin compounds, such as tributyltin (TBT), are used as biocides and antifouling agents in marine paints. However, they have been found to be toxic to aquatic life and are being phased out in many countries.

Phycobilins are linear tetrapyrrole chromophores found in cyanobacteria, red algae, and glaucophytes. They are the light-harvesting pigments associated with phycobiliproteins in the phycobilisome complex, which is a type of antenna system used to capture light for photosynthesis. The main types of phycobilins are phycocyanobilin, phycoerythrobilin, and allophycocyanobilin. These pigments absorb light in the blue-green to red region of the electromagnetic spectrum and transfer the energy to chlorophyll a for use in photosynthesis. Phycobilins are also used as fluorescent labels in various biochemical and medical research applications.

Ethylmorphine-N-demethylase is an enzyme that catalyzes the chemical reaction in the liver responsible for metabolizing (breaking down) the drug ethylmorphine. The enzyme does this by removing a methyl group from the ethylmorphine molecule, converting it into a different compound called normethadone. This enzyme is part of the cytochrome P450 family and is specifically classified as CYP2D6.

The activity of Ethylmorphine-N-demethylase (CYP2D6) can vary widely among individuals, which can affect how they metabolize certain drugs. Some people have multiple copies of the gene that encodes this enzyme and are considered "ultrarapid metabolizers," meaning they break down these drugs very quickly. Others may have reduced or even no activity of this enzyme due to genetic variations, which can lead to slower drug metabolism and potential for adverse effects.

I'm sorry for any confusion, but "Tin" does not have a medical definition. Tin is a chemical element with the symbol Sn and atomic number 50. It is a malleable, ductile, silvery-white post-transition metal. It is found in nature mainly as tin oxides and is obtained from the mineral cassiterite through mining and processing.

Tin has no known biological role in humans, animals, or plants, and it is not considered an essential nutrient. Small amounts of tin can be found in some foods and drinking water, but these levels are generally low and not considered harmful. High levels of tin can be toxic to the human body, causing symptoms such as nausea, vomiting, and diarrhea.

If you have any questions about a medical condition or treatment, I would recommend consulting with a healthcare professional for accurate information and guidance.

'Corynebacterium diphtheriae' is a gram-positive, rod-shaped, aerobic bacteria that can cause the disease diphtheria. It is commonly found in the upper respiratory tract and skin of humans and can be transmitted through respiratory droplets or direct contact with contaminated objects. The bacterium produces a potent exotoxin that can cause severe inflammation and formation of a pseudomembrane in the throat, leading to difficulty breathing and swallowing. In severe cases, the toxin can spread to other organs, causing serious complications such as myocarditis (inflammation of the heart muscle) and peripheral neuropathy (damage to nerves outside the brain and spinal cord). The disease is preventable through vaccination with the diphtheria toxoid-containing vaccine.

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.

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.

Hyperbilirubinemia is a medical condition characterized by an excessively high level of bilirubin in the bloodstream. Bilirubin is a yellowish pigment produced by the liver when it breaks down old red blood cells. Normally, bilirubin is conjugated (made water-soluble) in the liver and then excreted through the bile into the digestive system. However, if there is a problem with the liver's ability to process or excrete bilirubin, it can build up in the blood, leading to hyperbilirubinemia.

Hyperbilirubinemia can be classified as either unconjugated or conjugated, depending on whether the bilirubin is in its direct (conjugated) or indirect (unconjugated) form. Unconjugated hyperbilirubinemia can occur due to increased production of bilirubin (such as in hemolytic anemia), decreased uptake of bilirubin by the liver, or impaired conjugation of bilirubin in the liver. Conjugated hyperbilirubinemia, on the other hand, is usually caused by a problem with the excretion of conjugated bilirubin into the bile, such as in cholestatic liver diseases like hepatitis or cirrhosis.

Symptoms of hyperbilirubinemia can include jaundice (yellowing of the skin and eyes), dark urine, light-colored stools, itching, and fatigue. Treatment depends on the underlying cause of the condition and may involve medications, dietary changes, or surgery.

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.

Hemoglobinuria is a medical condition characterized by the presence of hemoglobin in the urine. Hemoglobin is a protein found in red blood cells that carries oxygen throughout the body. Normally, when red blood cells die, they are broken down and their hemoglobin is recycled. However, in certain conditions such as intravascular hemolysis (the destruction of red blood cells inside blood vessels), hemoglobin can be released into the bloodstream and then filtered by the kidneys into the urine.

Hemoglobinuria can be a symptom of various underlying medical conditions, including hemolytic anemias, disseminated intravascular coagulation (DIC), severe infections, snake bites, and exposure to certain toxins or medications. It is important to identify the underlying cause of hemoglobinuria, as treatment will depend on the specific condition.

In some cases, hemoglobinuria can lead to kidney damage due to the toxic effects of free hemoglobin on the renal tubules. This can result in acute or chronic kidney injury, and in severe cases, it may require dialysis or transplantation.

Microsomes, liver refers to a subcellular fraction of liver cells (hepatocytes) that are obtained during tissue homogenization and subsequent centrifugation. These microsomal fractions are rich in membranous structures known as the endoplasmic reticulum (ER), particularly the rough ER. They are involved in various important cellular processes, most notably the metabolism of xenobiotics (foreign substances) including drugs, toxins, and carcinogens.

The liver microsomes contain a variety of enzymes, such as cytochrome P450 monooxygenases, that are crucial for phase I drug metabolism. These enzymes help in the oxidation, reduction, or hydrolysis of xenobiotics, making them more water-soluble and facilitating their excretion from the body. Additionally, liver microsomes also host other enzymes involved in phase II conjugation reactions, where the metabolites from phase I are further modified by adding polar molecules like glucuronic acid, sulfate, or acetyl groups.

In summary, liver microsomes are a subcellular fraction of liver cells that play a significant role in the metabolism and detoxification of xenobiotics, contributing to the overall protection and maintenance of cellular homeostasis within the body.

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.

Oxidoreductases acting on CH-CH group donors are a class of enzymes within the larger group of oxidoreductases, which are responsible for catalyzing oxidation-reduction reactions. Specifically, this subclass of enzymes acts upon donors containing a carbon-carbon (CH-CH) bond, where one atom or group of atoms is oxidized and another is reduced during the reaction process. These enzymes play crucial roles in various metabolic pathways, including the breakdown and synthesis of carbohydrates, lipids, and amino acids.

The reactions catalyzed by these enzymes involve the transfer of electrons and hydrogen atoms between the donor and an acceptor molecule. This process often results in the formation or cleavage of carbon-carbon bonds, making them essential for numerous biological processes. The systematic name for this class of enzymes is typically structured as "donor:acceptor oxidoreductase," where donor and acceptor represent the molecules involved in the electron transfer process.

Examples of enzymes that fall under this category include:

1. Aldehyde dehydrogenases (EC 1.2.1.3): These enzymes catalyze the oxidation of aldehydes to carboxylic acids, using NAD+ as an electron acceptor.
2. Dihydrodiol dehydrogenase (EC 1.3.1.14): This enzyme is responsible for the oxidation of dihydrodiols to catechols in the biodegradation of aromatic compounds.
3. Succinate dehydrogenase (EC 1.3.5.1): A key enzyme in the citric acid cycle, succinate dehydrogenase catalyzes the oxidation of succinate to fumarate and reduces FAD to FADH2.
4. Xylose reductase (EC 1.1.1.307): This enzyme is involved in the metabolism of pentoses, where it reduces xylose to xylitol using NADPH as a cofactor.

Hemopexin is a protein found in blood plasma. It's primary function is to bind and transport heme, a potentially toxic molecule that is released when hemoglobin from red blood cells is broken down. Hemopexin helps to prevent damage to tissues and organs by keeping free heme levels low in the bloodstream. It also plays a role in the immune response and has antioxidant properties. A deficiency in hemopexin can lead to increased risk of tissue damage and inflammation.

Phycocyanin is a pigment-protein complex found in cyanobacteria and some types of algae, such as Spirulina. It belongs to the family of phycobiliproteins and plays a crucial role in the light-harvesting process during photosynthesis. Phycocyanin absorbs light in the orange and red regions of the visible spectrum and transfers the energy to chlorophyll for use in photosynthesis. It has been studied for its potential health benefits, including antioxidant, anti-inflammatory, and neuroprotective properties. However, more research is needed to fully understand its effects and potential therapeutic uses.

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.

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.

Rhodophyta, also known as red algae, is a division of simple, multicellular and complex marine algae. These organisms are characterized by their red pigmentation due to the presence of phycobiliproteins, specifically R-phycoerythrin and phycocyanin. They lack flagella and centrioles at any stage of their life cycle. The cell walls of Rhodophyta contain cellulose and various sulphated polysaccharides. Some species have calcium carbonate deposits in their cell walls, which contribute to the formation of coral reefs. Reproduction in these organisms is typically alternation of generations with a dominant gametophyte generation. They are an important source of food for many marine animals and have commercial value as well, particularly for the production of agar, carrageenan, and other products used in the food, pharmaceutical, and cosmetic industries.

Sodium compounds are chemical substances that contain the element sodium (Na) combined with one or more other elements. Sodium is an alkali metal and is highly reactive, so it rarely exists in its pure form in nature. Instead, it is typically found combined with other elements in the form of various sodium compounds.

Some common examples of sodium compounds include:

* Sodium chloride (NaCl), also known as table salt, which is a compound formed from the reaction between sodium and chlorine.
* Sodium bicarbonate (NaHCO3), also known as baking soda, which is used as a leavening agent in baking and as a household cleaner.
* Sodium hydroxide (NaOH), also known as lye, which is a strong alkali used in industrial applications such as the manufacture of soap and paper.
* Sodium carbonate (Na2CO3), also known as washing soda, which is used as a water softener and cleaning agent.

Sodium compounds have a variety of uses in medicine, including as electrolytes to help maintain fluid balance in the body, as antacids to neutralize stomach acid, and as laxatives to relieve constipation. However, it is important to use sodium compounds as directed by a healthcare professional, as excessive intake can lead to high blood pressure and other health problems.

Ferrochelatase is a medical/biochemical term that refers to an enzyme called Fe-chelatase or heme synthase. This enzyme plays a crucial role in the biosynthesis of heme, which is a vital component of hemoglobin, cytochromes, and other important biological molecules.

Ferrochelatase functions by catalyzing the insertion of ferrous iron (Fe2+) into protoporphyrin IX, the final step in heme biosynthesis. This enzyme is located within the inner mitochondrial membrane of cells and is widely expressed in various tissues, with particularly high levels found in erythroid precursor cells, liver, and brain.

Defects or mutations in the ferrochelatase gene can lead to a rare genetic disorder called erythropoietic protoporphyria (EPP), which is characterized by an accumulation of protoporphyrin IX in red blood cells, plasma, and other tissues. This accumulation results in photosensitivity, skin lesions, and potential complications such as liver dysfunction and gallstones.

Nuclear factor erythroid-derived 2-like 2 (NFE2L2), also known as NF-E2-related factor 2 (NRF2), is a protein that plays a crucial role in the regulation of cellular responses to oxidative stress and electrophilic substances. It is a transcription factor that binds to the antioxidant response element (ARE) in the promoter region of various genes, inducing their expression and promoting cellular defense against harmful stimuli.

Under normal conditions, NRF2 is bound to its inhibitor, Kelch-like ECH-associated protein 1 (KEAP1), in the cytoplasm, where it is targeted for degradation by the proteasome. However, upon exposure to oxidative stress or electrophilic substances, KEAP1 undergoes conformational changes, leading to the release and stabilization of NRF2. Subsequently, NRF2 translocates to the nucleus, forms a complex with small Maf proteins, and binds to AREs, inducing the expression of genes involved in antioxidant response, detoxification, and cellular protection.

Genetic variations or dysregulation of the NFE2L2/KEAP1 pathway have been implicated in several diseases, including cancer, neurodegenerative disorders, and pulmonary fibrosis, highlighting its importance in maintaining cellular homeostasis and preventing disease progression.

Allylisopropylacetamide is not a term that has a widely accepted or established medical definition. It is a chemical compound with the formula (CH₂CHCH₂)N(C=O)CH(CH₃)₂, and it may have various chemical or industrial uses, but it is not a term that is commonly used in medical contexts.

If you have any specific questions about this compound or its potential uses or effects, I would recommend consulting with a relevant expert, such as a chemist or toxicologist, who can provide more detailed and accurate information based on their expertise and knowledge of the subject.

Porphobilinogen Synthase (also known as PBGD or hydroxymethylbilane synthase) is an enzyme that catalyzes the second step in the heme biosynthesis pathway. This enzyme is responsible for converting two molecules of porphobilinogen into a linear tetrapyrrole called hydroxymethylbilane, which is then converted into uroporphyrinogen III by uroporphyrinogen III synthase.

Deficiency in Porphobilinogen Synthase can lead to a rare genetic disorder known as acute intermittent porphyria (AIP), which is characterized by the accumulation of porphobilinogen and other precursors in the heme biosynthesis pathway, resulting in neurovisceral symptoms such as abdominal pain, vomiting, neuropathy, and psychiatric disturbances.

The Cytochrome P-450 (CYP450) enzyme system is a group of enzymes found primarily in the liver, but also in other organs such as the intestines, lungs, and skin. These enzymes play a crucial role in the metabolism and biotransformation of various substances, including drugs, environmental toxins, and endogenous compounds like hormones and fatty acids.

The name "Cytochrome P-450" refers to the unique property of these enzymes to bind to carbon monoxide (CO) and form a complex that absorbs light at a wavelength of 450 nm, which can be detected spectrophotometrically.

The CYP450 enzyme system is involved in Phase I metabolism of xenobiotics, where it catalyzes oxidation reactions such as hydroxylation, dealkylation, and epoxidation. These reactions introduce functional groups into the substrate molecule, which can then undergo further modifications by other enzymes during Phase II metabolism.

There are several families and subfamilies of CYP450 enzymes, each with distinct substrate specificities and functions. Some of the most important CYP450 enzymes include:

1. CYP3A4: This is the most abundant CYP450 enzyme in the human liver and is involved in the metabolism of approximately 50% of all drugs. It also metabolizes various endogenous compounds like steroids, bile acids, and vitamin D.
2. CYP2D6: This enzyme is responsible for the metabolism of many psychotropic drugs, including antidepressants, antipsychotics, and beta-blockers. It also metabolizes some endogenous compounds like dopamine and serotonin.
3. CYP2C9: This enzyme plays a significant role in the metabolism of warfarin, phenytoin, and nonsteroidal anti-inflammatory drugs (NSAIDs).
4. CYP2C19: This enzyme is involved in the metabolism of proton pump inhibitors, antidepressants, and clopidogrel.
5. CYP2E1: This enzyme metabolizes various xenobiotics like alcohol, acetaminophen, and carbon tetrachloride, as well as some endogenous compounds like fatty acids and prostaglandins.

Genetic polymorphisms in CYP450 enzymes can significantly affect drug metabolism and response, leading to interindividual variability in drug efficacy and toxicity. Understanding the role of CYP450 enzymes in drug metabolism is crucial for optimizing pharmacotherapy and minimizing adverse effects.

Aminolevulinic acid (ALA) is a naturally occurring compound in the human body and is a key precursor in the biosynthesis of heme, which is a component of hemoglobin in red blood cells. It is also used as a photosensitizer in dermatology for the treatment of certain types of skin conditions such as actinic keratosis and basal cell carcinoma.

In medical terms, ALA is classified as an α-keto acid and a porphyrin precursor. It is synthesized in the mitochondria from glycine and succinyl-CoA in a reaction catalyzed by the enzyme aminolevulinic acid synthase. After its synthesis, ALA is transported to the cytosol where it undergoes further metabolism to form porphyrins, which are then used for heme biosynthesis in the mitochondria.

In dermatology, topical application of ALA followed by exposure to a specific wavelength of light can lead to the production of reactive oxygen species that destroy abnormal cells in the skin while leaving healthy cells unharmed. This makes it an effective treatment for precancerous and cancerous lesions on the skin.

It is important to note that ALA can cause photosensitivity, which means that patients who have undergone ALA-based treatments should avoid exposure to sunlight or other sources of bright light for a period of time after the treatment to prevent adverse reactions.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

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.

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.

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.

Myoglobin is a protein found in the muscle tissue, particularly in red or skeletal muscles. It belongs to the globin family and has a similar structure to hemoglobin, another oxygen-binding protein found in red blood cells. Myoglobin's primary function is to store oxygen within the muscle cells, making it readily available for use during periods of increased oxygen demand, such as during physical exertion.

Myoglobin contains heme groups that bind to and release oxygen molecules. The protein has a higher affinity for oxygen than hemoglobin, allowing it to maintain its bound oxygen even in low-oxygen environments. When muscle cells are damaged or undergo necrosis (cell death), myoglobin is released into the bloodstream and can be detected in serum or urine samples. Elevated levels of myoglobin in the blood or urine may indicate muscle injury, trauma, or diseases affecting muscle integrity, such as rhabdomyolysis or muscular dystrophies.

Hemoglobin (Hb or Hgb) is the main oxygen-carrying protein in the red blood cells, which are responsible for delivering oxygen throughout the body. It is a complex molecule made up of four globin proteins and four heme groups. Each heme group contains an iron atom that binds to one molecule of oxygen. Hemoglobin plays a crucial role in the transport of oxygen from the lungs to the body's tissues, and also helps to carry carbon dioxide back to the lungs for exhalation.

There are several types of hemoglobin present in the human body, including:

* Hemoglobin A (HbA): This is the most common type of hemoglobin, making up about 95-98% of total hemoglobin in adults. It consists of two alpha and two beta globin chains.
* Hemoglobin A2 (HbA2): This makes up about 1.5-3.5% of total hemoglobin in adults. It consists of two alpha and two delta globin chains.
* Hemoglobin F (HbF): This is the main type of hemoglobin present in fetal life, but it persists at low levels in adults. It consists of two alpha and two gamma globin chains.
* Hemoglobin S (HbS): This is an abnormal form of hemoglobin that can cause sickle cell disease when it occurs in the homozygous state (i.e., both copies of the gene are affected). It results from a single amino acid substitution in the beta globin chain.
* Hemoglobin C (HbC): This is another abnormal form of hemoglobin that can cause mild to moderate hemolytic anemia when it occurs in the homozygous state. It results from a different single amino acid substitution in the beta globin chain than HbS.

Abnormal forms of hemoglobin, such as HbS and HbC, can lead to various clinical disorders, including sickle cell disease, thalassemia, and other hemoglobinopathies.

Arsenites are inorganic compounds that contain arsenic in the trivalent state (arsenic-III). They are formed by the reaction of arsenic trioxide (As2O3) or other trivalent arsenic compounds with bases such as sodium hydroxide, potassium hydroxide, or ammonia.

The most common and well-known arsenite is sodium arsenite (NaAsO2), which has been used in the past as a wood preservative and pesticide. However, due to its high toxicity and carcinogenicity, its use has been largely discontinued. Other examples of arsenites include potassium arsenite (KAsO2) and calcium arsenite (Ca3(AsO3)2).

Arsenites are highly toxic and can cause a range of health effects, including skin irritation, nausea, vomiting, diarrhea, abdominal pain, and death in severe cases. Long-term exposure to arsenites has been linked to an increased risk of cancer, particularly lung, bladder, and skin cancer.

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.

Enzyme inhibitors are substances that bind to an enzyme and decrease its activity, preventing it from catalyzing a chemical reaction in the body. They can work by several mechanisms, including blocking the active site where the substrate binds, or binding to another site on the enzyme to change its shape and prevent substrate binding. Enzyme inhibitors are often used as drugs to treat various medical conditions, such as high blood pressure, abnormal heart rhythms, and bacterial infections. They can also be found naturally in some foods and plants, and can be used in research to understand enzyme function and regulation.

Nitric oxide (NO) is a molecule made up of one nitrogen atom and one oxygen atom. In the body, it is a crucial signaling molecule involved in various physiological processes such as vasodilation, immune response, neurotransmission, and inhibition of platelet aggregation. It is produced naturally by the enzyme nitric oxide synthase (NOS) from the amino acid L-arginine. Inhaled nitric oxide is used medically to treat pulmonary hypertension in newborns and adults, as it helps to relax and widen blood vessels, improving oxygenation and blood flow.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

Microsomes are subcellular membranous vesicles that are obtained as a byproduct during the preparation of cellular homogenates. They are not naturally occurring structures within the cell, but rather formed due to fragmentation of the endoplasmic reticulum (ER) during laboratory procedures. Microsomes are widely used in various research and scientific studies, particularly in the fields of biochemistry and pharmacology.

Microsomes are rich in enzymes, including the cytochrome P450 system, which is involved in the metabolism of drugs, toxins, and other xenobiotics. These enzymes play a crucial role in detoxifying foreign substances and eliminating them from the body. As such, microsomes serve as an essential tool for studying drug metabolism, toxicity, and interactions, allowing researchers to better understand and predict the effects of various compounds on living organisms.

Ribulose phosphates are organic compounds that play a crucial role in the Calvin cycle, which is a part of photosynthesis. The Calvin cycle is the process by which plants, algae, and some bacteria convert carbon dioxide into glucose and other simple sugars.

Ribulose phosphates are sugar phosphates that contain five carbon atoms and have the chemical formula C5H10O5P. They exist in two forms: ribulose 5-phosphate (Ru5P) and ribulose 1,5-bisphosphate (RuBP).

Ribulose 1,5-bisphosphate is the starting point for carbon fixation in the Calvin cycle. In this process, an enzyme called RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyzes the reaction between RuBP and carbon dioxide to form two molecules of 3-phosphoglycerate, which are then converted into glucose and other sugars.

Ribulose phosphates are also involved in other metabolic pathways, such as the pentose phosphate pathway, which generates reducing power in the form of NADPH and produces ribose-5-phosphate, a precursor for nucleotide synthesis.

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.

Dioxygenases are a class of enzymes that catalyze the incorporation of both atoms of molecular oxygen (O2) into their substrates. They are classified based on the type of reaction they catalyze and the number of iron atoms in their active site. The two main types of dioxygenases are:

1. Intradiol dioxygenases: These enzymes cleave an aromatic ring by inserting both atoms of O2 into a single bond between two carbon atoms, leading to the formation of an unsaturated diol (catechol) intermediate and the release of CO2. They contain a non-heme iron(III) center in their active site.

An example of intradiol dioxygenase is catechol 1,2-dioxygenase, which catalyzes the conversion of catechol to muconic acid.

2. Extradiol dioxygenases: These enzymes cleave an aromatic ring by inserting one atom of O2 at a position adjacent to the hydroxyl group and the other atom at a more distant position, leading to the formation of an unsaturated lactone or cyclic ether intermediate. They contain a non-heme iron(II) center in their active site.

An example of extradiol dioxygenase is homogentisate 1,2-dioxygenase, which catalyzes the conversion of homogentisate to maleylacetoacetate in the tyrosine degradation pathway.

Dioxygenases play important roles in various biological processes, including the metabolism of aromatic compounds, the biosynthesis of hormones and signaling molecules, and the detoxification of xenobiotics.

Methaemalbumin is not a term that has a widely accepted or established medical definition. It's possible that you may be referring to "methaemoglobin," which is related to hemoglobin, a protein in red blood cells that carries oxygen throughout the body.

Methaemoglobin (MetHb) is a form of hemoglobin in which the iron within the heme group is in the ferric (Fe3+) state instead of the ferrous (Fe2+) state, making it unable to bind and transport oxygen effectively. This can occur due to exposure to certain chemicals or drugs, genetic conditions, or metabolic disorders.

If you meant something else by 'methemalbumin,' I would recommend consulting a medical professional or looking up the term in a reputable medical dictionary for clarification.

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.

Sprague-Dawley rats are a strain of albino laboratory rats that are widely used in scientific research. They were first developed by researchers H.H. Sprague and R.C. Dawley in the early 20th century, and have since become one of the most commonly used rat strains in biomedical research due to their relatively large size, ease of handling, and consistent genetic background.

Sprague-Dawley rats are outbred, which means that they are genetically diverse and do not suffer from the same limitations as inbred strains, which can have reduced fertility and increased susceptibility to certain diseases. They are also characterized by their docile nature and low levels of aggression, making them easier to handle and study than some other rat strains.

These rats are used in a wide variety of research areas, including toxicology, pharmacology, nutrition, cancer, and behavioral studies. Because they are genetically diverse, Sprague-Dawley rats can be used to model a range of human diseases and conditions, making them an important tool in the development of new drugs and therapies.

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.

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.

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.

Ferritin is a protein in iron-metabolizing cells that stores iron in a water-soluble form. It is found inside the cells (intracellular) and is released into the bloodstream when the cells break down or die. Measuring the level of ferritin in the blood can help determine the amount of iron stored in the body. High levels of ferritin may indicate hemochromatosis, inflammation, liver disease, or other conditions. Low levels of ferritin may indicate anemia, iron deficiency, or other conditions.

Nitric Oxide Synthase (NOS) is a group of enzymes that catalyze the production of nitric oxide (NO) from L-arginine. There are three distinct isoforms of NOS, each with different expression patterns and functions:

1. Neuronal Nitric Oxide Synthase (nNOS or NOS1): This isoform is primarily expressed in the nervous system and plays a role in neurotransmission, synaptic plasticity, and learning and memory processes.
2. Inducible Nitric Oxide Synthase (iNOS or NOS2): This isoform is induced by various stimuli such as cytokines, lipopolysaccharides, and hypoxia in a variety of cells including immune cells, endothelial cells, and smooth muscle cells. iNOS produces large amounts of NO, which functions as a potent effector molecule in the immune response, particularly in the defense against microbial pathogens.
3. Endothelial Nitric Oxide Synthase (eNOS or NOS3): This isoform is constitutively expressed in endothelial cells and produces low levels of NO that play a crucial role in maintaining vascular homeostasis by regulating vasodilation, inhibiting platelet aggregation, and preventing smooth muscle cell proliferation.

Overall, NOS plays an essential role in various physiological processes, including neurotransmission, immune response, cardiovascular function, and respiratory regulation. Dysregulation of NOS activity has been implicated in several pathological conditions such as hypertension, atherosclerosis, neurodegenerative diseases, and inflammatory disorders.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

A kidney, in medical terms, is one of two bean-shaped organs located in the lower back region of the body. They are essential for maintaining homeostasis within the body by performing several crucial functions such as:

1. Regulation of water and electrolyte balance: Kidneys help regulate the amount of water and various electrolytes like sodium, potassium, and calcium in the bloodstream to maintain a stable internal environment.

2. Excretion of waste products: They filter waste products from the blood, including urea (a byproduct of protein metabolism), creatinine (a breakdown product of muscle tissue), and other harmful substances that result from normal cellular functions or external sources like medications and toxins.

3. Endocrine function: Kidneys produce several hormones with important roles in the body, such as erythropoietin (stimulates red blood cell production), renin (regulates blood pressure), and calcitriol (activated form of vitamin D that helps regulate calcium homeostasis).

4. pH balance regulation: Kidneys maintain the proper acid-base balance in the body by excreting either hydrogen ions or bicarbonate ions, depending on whether the blood is too acidic or too alkaline.

5. Blood pressure control: The kidneys play a significant role in regulating blood pressure through the renin-angiotensin-aldosterone system (RAAS), which constricts blood vessels and promotes sodium and water retention to increase blood volume and, consequently, blood pressure.

Anatomically, each kidney is approximately 10-12 cm long, 5-7 cm wide, and 3 cm thick, with a weight of about 120-170 grams. They are surrounded by a protective layer of fat and connected to the urinary system through the renal pelvis, ureters, bladder, and urethra.

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.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Etiolation is a medical term that refers to the abnormal physical development of a plant due to insufficient exposure to light. This results in elongated, weak stems, reduced leaf size and sometimes pale green or yellowish leaves because the plant is trying to grow towards the light source. It can also reduce the amount of chlorophyll produced by the plant, which affects its ability to photosynthesize. Etiolation is not a disease but rather a physiological response to inadequate light conditions.

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.

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.

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.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Phytochrome is a photoreceptor protein responsible for detecting and mediating responses to different wavelengths of light, primarily red and far-red, in plants and some microorganisms. It plays a crucial role in various physiological processes such as seed germination, stem elongation, leaf expansion, chlorophyll production, and flowering.

The phytochrome protein exists in two interconvertible forms: Pr (the red-light-absorbing form) and Pfr (the far-red-light-absorbing form). The conversion between these forms regulates the downstream signaling pathways that control plant growth and development. Red light (around 660 nm) promotes the formation of the Pfr form, while far-red light (around 730 nm) converts it back to the Pr form. This reversible photoresponse allows plants to adapt their growth patterns based on the quality and duration of light they receive.

... heme oxygenase (decyclizing) MeSH D08.811.682.690.708.410.500 - heme oxygenase-1 MeSH D08.811.682.690.708.425 - 4- ... tryptophan oxygenase MeSH D08.811.682.690.562 - inositol oxygenase MeSH D08.811.682.690.708 - mixed function oxygenases MeSH ...
Muller R, Schmitt S, Lingens F (1982). "A novel non-heme iron-containing dioxygenase. Chloridazon-catechol dioxygenase from ... oxygenases). The oxygen incorporated need not be derived from O2. The systematic name of this enzyme class is 5-amino-4-chloro- ... 2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone 1,2-oxidoreductase (decyclizing). It employs one cofactor, iron. Muller R, Haug S, ...
... it is synthesized endogenously by heme oxygenase type 1 (Ho-1) in response to ischemic stress. Ho-1-deficient (Hmox1-/-) mice ... Heme Oxygenase (Decyclizing) Grants and funding * R01 HL55397/HL/NHLBI NIH HHS/United States ... Carbon monoxide (CO) can arrest cellular respiration, but paradoxically, it is synthesized endogenously by heme oxygenase type ...
... heme oxygenase (decyclizing) MeSH D08.811.682.690.708.410.500 - heme oxygenase-1 MeSH D08.811.682.690.708.425 - 4- ... tryptophan oxygenase MeSH D08.811.682.690.562 - inositol oxygenase MeSH D08.811.682.690.708 - mixed function oxygenases MeSH ...
Heme Oxygenase (Decyclizing), 1.14.99.3; Hmox1 protein, rat, 1.14.99.3; Losartan, 114798-26-4; Minoxidil, 38304-91-5; NADPH ... Heme Oxygenase (Decyclizing); Hypertension, Renal; Losartan; Male; Minoxidil; NADPH Oxidase; Oxidative Stress; Rats; Rats, ... Maines, M.D., Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications (1988) FASEB J, 2, pp. ... Polizio, A.H., Gonzales, S., Muñoz, M.C., Behaviour of the anti-oxidant defense system and heme oxygenase-1 protein expression ...
Heme Oxygenase (Decyclizing) Medicine & Life Sciences 37% * Nitric Oxide Medicine & Life Sciences 37% ... keywords = "Apis, Cystathionine β-synthase, Heme oxygenase, Nitric oxide synthase, Soluble guanylyl cyclase", ... and heme oxygenase (HO) from the honeybee brain. The honeybee brain contains at least one gene for each of NOS, CBS, and HO. ... and heme oxygenase (HO) from the honeybee brain. The honeybee brain contains at least one gene for each of NOS, CBS, and HO. ...
Heme Oxygenase (Decyclizing) * Large-Conductance Calcium-Activated Potassium Channels * Male * Organometallic Compounds ... Regulation of endothelial BK channels by heme oxygenase-derived carbon monoxide and caveolin-1. Academic Article * ... Previously, we demonstrated that inhibition of either BK channels or heme oxygenase (HO) restores vasoconstrictor reactivity ...
Paclitaxel Protects against Isoproterenol-Induced Damage in Rat Myocardium: Its Heme-Oxygenase Mediated Role in Cardiovascular ...
heme oxygenase (decyclizing) activity. IEP. Enrichment. MF. GO:0004784. superoxide dismutase activity. IEP. Enrichment. ...
Heme Oxygenase (Decyclizing) 95% * Foam Cells 88% * ATP-Binding Cassette Transporters 84% ... EGb761 ameliorates the formation of foam cells by regulating the expression of SR-A and ABCA1: Role of haem oxygenase-1. Tsai, ...
heme oxygenase (decyclizing) activity. IEP. Enrichment. MF. GO:0004635. phosphoribosyl-AMP cyclohydrolase activity. IEP. ...
Heme Oxygenase-1 100% * Immune System Diseases 90% * Heme Oxygenase (Decyclizing) 16% ... Heme oxygenase-1 as a modulator of intestinal inflammation development and progression. Sebastián, V. P., Salazar, G. A., ... Naturally Derived Heme-Oxygenase 1 Inducers and Their Therapeutic Application to Immune-Mediated Diseases. Funes, S. C., Rios, ...
heme oxygenase (decyclizing) activity GO:0004392 * oxidoreductase activity GO:0052584 * 2,3-bis(4-hydroxyphenyl)-1,2- ...
enables heme oxygenase (decyclizing) activity IBA Inferred from Biological aspect of Ancestor. more info ... Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. HMOX1 and HMOX2 belong ... Heme oxygenase 1 in erythropoiesis: an important regulator beyond catalyzing heme catabolism. Title: Heme oxygenase 1 in ... heme oxygenase 1. Names. heat shock protein, 32-kD. heme oxygenase (decycling) 1. NP_002124.1. *EC 1.14.14.18 ...
Oxygenases [D08.811.682.690]. *Mixed Function Oxygenases [D08.811.682.690.708]. *Heme Oxygenase (Decyclizing) [D08.811.682.690. ... "Heme Oxygenase-1" by people in UAMS Profiles by year, and whether "Heme Oxygenase-1" was a major or minor topic of these ... "Heme Oxygenase-1" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject ... Leal EC, Carvalho E. Heme Oxygenase-1 as Therapeutic Target for Diabetic Foot Ulcers. Int J Mol Sci. 2022 Oct 10; 23(19). ...
Heme Oxygenase (Decyclizing) Medicine & Life Sciences 26% * FE 999049 Medicine & Life Sciences 22% ...
Heme Oxygenase (Decyclizing) Medicine & Life Sciences 100% * Nitric Oxide Synthase Medicine & Life Sciences 71% ... Carbon monoxide is generated by heme oxygenase (HO), an enzyme inducible by heme, cytokines, and oxidative stress and ... Carbon monoxide is generated by heme oxygenase (HO), an enzyme inducible by heme, cytokines, and oxidative stress and ... Carbon monoxide is generated by heme oxygenase (HO), an enzyme inducible by heme, cytokines, and oxidative stress and ...
Heme Oxygenase (Decyclizing) Medicine & Life Sciences 54% * Oxidative Stress Medicine & Life Sciences 49% ... Tsc1GFAP−/− mice expressed more microRNA-155 and haem oxygenase 1 in the brain compared to wild-type, preceding the typical ... Tsc1GFAP−/− mice expressed more microRNA-155 and haem oxygenase 1 in the brain compared to wild-type, preceding the typical ... Tsc1GFAP−/− mice expressed more microRNA-155 and haem oxygenase 1 in the brain compared to wild-type, preceding the typical ...
Oxygenases Medicine & Life Sciences 15% * Heme Oxygenase (Decyclizing) Medicine & Life Sciences 15% ... This study aimed to investigate whether carbon monoxide (CO), a product of heme oxygenase that degrades protoheme IX, serves as ... N2 - This study aimed to investigate whether carbon monoxide (CO), a product of heme oxygenase that degrades protoheme IX, ... AB - This study aimed to investigate whether carbon monoxide (CO), a product of heme oxygenase that degrades protoheme IX, ...
Heme Oxygenase (Decyclizing) Medicine & Life Sciences 85% * Citric Acid Cycle Medicine & Life Sciences 29% ... Haem oxygenase is synthetically lethal with the tumour suppressor fumarate hydratase. In: Nature. 2011 ; Vol. 477, No. 7363. pp ... Haem oxygenase is synthetically lethal with the tumour suppressor fumarate hydratase. Nature. 2011 Sep 8;477(7363):225-228. doi ... Haem oxygenase is synthetically lethal with the tumour suppressor fumarate hydratase. Christian Frezza, Liang Zheng, Ori Folger ...
Heme Oxygenase (Decyclizing). *Kynurenine 3-Monooxygenase. *Phenylalanine Hydroxylase. *Procollagen-Lysine, 2-Oxoglutarate 5- ...
... while the heme oxygenase 2 haplotype is protective against the onset of the syndrome. Such data support further previous ... Secondly, a common haplotype in the heme oxygenase 2 gene was reduced in patients with ARDS compared to healthy control ... Heme Oxygenase (Decyclizing), Homeostasis, Humans, Iron, Male, Middle Aged, Multicenter Studies as Topic, Polymorphism, Single ... Secondly, a common haplotype in the heme oxygenase 2 gene was reduced in patients with ARDS compared to healthy control ...
Heme, Heme Oxygenase (Decyclizing), Kidney Neoplasms, Leiomyomatosis, Mice, Mitochondria, Mutation, NAD, Neoplastic Syndromes, ... Haem oxygenase is synthetically lethal with the tumour suppressor fumarate hydratase. Frezza C., Zheng L., Folger O., ...
Decyclizing heme oxygenase inhibitors, Immunomodulators, Virus replication inhibitors, CD28 antigen modulators, ...
... while the heme oxygenase 2 haplotype is protective against the onset of the syndrome. Such data support further previous ... Secondly, a common haplotype in the heme oxygenase 2 gene was reduced in patients with ARDS compared to healthy control ... Heme Oxygenase (Decyclizing), Homeostasis, Humans, Iron, Male, Middle Aged, Multicenter Studies as Topic, Polymorphism, Single ... Secondly, a common haplotype in the heme oxygenase 2 gene was reduced in patients with ARDS compared to healthy control ...
Decyclizing heme oxygenase inhibitors, Immunomodulators, Virus replication inhibitors, CD28 antigen modulators, ...
heme oxygenase (decyclizing) 1 Chromosome:. 22 (View: 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 X Y MT). ...
Heme Oxygenase (Decyclizing) [D08.811.682.690.708.410] Heme Oxygenase (Decyclizing) * 4-Hydroxybenzoate-3-Monooxygenase [ ... 2006; TRANS-CINNAMATE 4-MONOOXYGENASE was indexed under CYTOCHROME P-450 ENZYME SYSTEM & MIXED FUNCTION OXYGENASES 1983-2005 ...
Heme Oxygenase (Decyclizing):metabolism, Heme Oxygenase-1, Humans, Immunohistochemistry, Membrane Proteins, Middle Aged, ... The presence of heme-oxygenase and biliverdin reductase in human cranial ganglia indicates a role for carbon monoxide in neural ... Uddman R, Tajti J, Sundler F, Cardell L. The presence of heme-oxygenase and biliverdin reductase in human cranial ganglia ...
Heme Oxygenase-1. *Antiviral Agents. *Hepacivirus. *Heme Oxygenase (Decyclizing). *Hepatitis C, Chronic ...
Heme Oxygenase (Decyclizing). *Kynurenine 3-Monooxygenase. *Phenylalanine Hydroxylase. *Procollagen-Lysine, 2-Oxoglutarate 5- ...
  • Thoracic aortic segments were excised, and the NAD(P)H oxidase subunits expression, oxidative stress parameters, and heme oxygenase-1 abundance were evaluated. (uba.ar)
  • Hypoxia-induced oxidative stress promotes therapy resistance via upregulation of heme oxygenase-1 in multiple myeloma. (nih.gov)
  • Methods: We investigated oxidative stress markers, including haem oxygenase 1, ferritin and the inflammation associated microRNA-155 in surgically resected epileptogenic brain tissue of TSC (n = 10) and FCD IIb (n = 8) patients and in a TSC model (Tsc1 GFAP−/− mice) using immunohistochemistry, in situ hybridization, real-time quantitative PCR and immunoblotting. (wustl.edu)
  • In vitro, chronic microRNA-155 overexpression induced haem oxygenase 1, iron regulatory elements and increased susceptibility to oxidative stress. (wustl.edu)
  • In the present study, we identified the genes of nitric oxide synthase (NOS), soluble guanylyl cyclase (sGC), cystathionine β-synthase (CBS), and heme oxygenase (HO) from the honeybee brain. (elsevierpure.com)
  • HMOX1 and HMOX2 belong to the heme oxygenase family. (nih.gov)
  • Heme oxygenase, an essential enzyme in heme catabolism, cleaves heme to form biliverdin, which is subsequently converted to bilirubin by biliverdin reductase, and carbon monoxide, a putative neurotransmitter. (nih.gov)
  • The presence of heme-oxygenase and biliverdin reductase in human cranial ganglia indicates a role for carbon monoxide in neural transmission. (nel.edu)
  • Heme oxygenase occurs as 2 isozymes, an inducible heme oxygenase-1 and a constitutive heme oxygenase-2. (nih.gov)
  • Renal intramedullary infusion of tempol normalizes the blood pressure?response to intrarenal blockade of heme oxygenase-1 in?angiotensin II-dependent hypertension. (uams.edu)
  • Tsc1 GFAP−/− mice expressed more microRNA-155 and haem oxygenase 1 in the brain compared to wild-type, preceding the typical development of spontaneous seizures in these animals. (wustl.edu)
  • Carbon monoxide (CO) can arrest cellular respiration, but paradoxically, it is synthesized endogenously by heme oxygenase type 1 (Ho-1) in response to ischemic stress. (nih.gov)
  • Regulation of endothelial BK channels by heme oxygenase-derived carbon monoxide and caveolin-1. (unm.edu)
  • This study aimed to investigate whether carbon monoxide (CO), a product of heme oxygenase that degrades protoheme IX, serves as an endogenous modulator for biliary transport. (elsevierpure.com)
  • CONCLUSIONS: These results provide preliminary evidence to suggest a distinction in the genetic background of the subpopulations studied, inferring that the ferritin light-chain gene genotype confers susceptibility to ARDS, while the heme oxygenase 2 haplotype is protective against the onset of the syndrome. (ox.ac.uk)
  • Previously, we demonstrated that inhibition of either BK channels or heme oxygenase (HO) restores vasoconstrictor reactivity after CH. Additionally, administration of the scaffolding domain of caveolin (Cav)-1 inhibits EC BK activity and restores vasoconstrictor reactivity in this setting. (unm.edu)
  • Heme oxygenase activity is induced by its substrate heme and by various nonheme substances. (nih.gov)
  • Human Heme Oxygenase-1 Promoter Activity Is Mediated by Z-DNA Formation. (nih.gov)
  • Association between heme oxygenase one and sepsis development in patients with moderate-to-critical COVID-19: a single-center, retrospective observational study. (nih.gov)
  • Secondly, a common haplotype in the heme oxygenase 2 gene was reduced in patients with ARDS compared to healthy control subjects and was more evident in those with ARDS of direct or pulmonary etiology. (ox.ac.uk)
  • Haem oxygenase (HO) enzyme and the pro-inflammatory cytokine tumour necrosis factor (TNF) have been proposed as one of the factors that may play significant role in pathogenicity/severity of malaria infection. (nih.gov)
  • PCC 6803 heme oxygenase encoded by ho1 can substitute for the defective HY1 gene product and that the only required enzyme activity of the HY1 gene product is heme oxygenase. (edu.au)
  • Evidence is presented which suggests that NO stimulates GnRH release due to its ability to modulate the heme-containing enzyme, guanylate cyclase, which leads to enhanced production of the second messenger molecule, cGMP. (elsevierpure.com)
  • Regulation of endothelial BK channels by heme oxygenase-derived carbon monoxide and caveolin-1. (unm.edu)
  • Tin(IV) protoporphyrin IX (Sn-protoporphyrin) potently inhibits heme degradation to bilirubin in vitro and in vivo, and it completely suppresses neonatal hyperbilirubinemia in experimental animals, including primates. (utmb.edu)
  • We have examined in this study the fate of that fraction of heme whose degradation to bile pigment is inhibited in vivo by administration of this heme oxygenase (EC 1.14.99.3) inhibitor. (utmb.edu)
  • CO may also play a role in stimulating GnRH secretion as heme molecules stimulate GnRH release in vitro, an effect which requires heme oxygenase activity and is blocked by the gaseous scavenger molecule, hemoglobin. (elsevierpure.com)
  • A heme oxygenase-encoding gene, ho1, was recently cloned from the cyanobacterium Synechocystis sp. (edu.au)
  • Sn-protoporphyrin, administered with the exogenous heme, markedly increased (3- to 4-fold) the amount of heme excreted into bile and greatly diminished biliary output of bilirubin. (utmb.edu)
  • The increase in biliary heme output exceeded the decrease in bilirubin excretion elicited by the inhibitor metalloporphyrin. (utmb.edu)
  • This decrease in biliary bilirubin output was accounted for entirely by a prompt and marked increase in biliary excretion of unmetabolized heme. (utmb.edu)
  • The enhanced biliary excretion of unmetabolized heme following administration of Sn-protoporphyrin is a newly defined and biologically important response associated with use of this synthetic heme analogue. (utmb.edu)