Peroxidases that utilize ASCORBIC ACID as an electron donor to reduce HYDROGEN PEROXIDE to WATER. The reaction results in the production of monodehydroascorbic acid and DEHYDROASCORBIC ACID.
Peroxidases are enzymes that catalyze the reduction of hydrogen peroxide to water, while oxidizing various organic and inorganic compounds, playing crucial roles in diverse biological processes including stress response, immune defense, and biosynthetic reactions.
An enzyme that converts ascorbic acid to dehydroascorbic acid. EC
A six carbon compound related to glucose. It is found naturally in citrus fruits and many vegetables. Ascorbic acid is an essential nutrient in human diets, and necessary to maintain connective tissue and bone. Its biologically active form, vitamin C, functions as a reducing agent and coenzyme in several metabolic pathways. Vitamin C is considered an antioxidant.
An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.
An enzyme catalyzing the oxidation of 2 moles of glutathione in the presence of hydrogen peroxide to yield oxidized glutathione and water. EC
A hemeprotein which catalyzes the oxidation of ferrocytochrome c to ferricytochrome c in the presence of hydrogen peroxide. EC
An agent thought to have disinfectant properties and used as an expectorant. (From Martindale, The Extra Pharmacopoeia, 30th ed, p747)
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.
A hemeprotein from leukocytes. Deficiency of this enzyme leads to a hereditary disorder coupled with disseminated moniliasis. It catalyzes the conversion of a donor and peroxide to an oxidized donor and water. EC
An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA.
Proteins encoded by the CHLOROPLAST GENOME or proteins encoded by the nuclear genome that are imported to and resident in the CHOROPLASTS.
Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.
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.
Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC
A widely cultivated plant, native to Asia, having succulent, edible leaves eaten as a vegetable. (From American Heritage Dictionary, 1982)
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 variable annual leguminous vine (Pisum sativum) that is cultivated for its rounded smooth or wrinkled edible protein-rich seeds, the seed of the pea, and the immature pods with their included seeds. (From Webster's New Collegiate Dictionary, 1973)
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
An oxidoreductase that catalyzes the reaction between superoxide anions and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. EC
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
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).
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A 66-kDa peroxidase found in EOSINOPHIL granules. Eosinophil peroxidase is a cationic protein with a pI of 10.8 and is comprised of a heavy chain subunit and a light chain subunit. It possesses cytotoxic activity towards BACTERIA and other organisms, which is attributed to its peroxidase activity.
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
The reversibly oxidized form of ascorbic acid. It is the lactone of 2,3-DIKETOGULONIC ACID and has antiscorbutic activity in man on oral ingestion.
Prolonged dry periods in natural climate cycle. They are slow-onset phenomena caused by rainfall deficit combined with other predisposing factors.
A plant genus of the family SOLANACEAE. Members contain NICOTINE and other biologically active chemicals; its dried leaves are used for SMOKING.
A hemeprotein that catalyzes the oxidation of the iodide radical to iodine with the subsequent iodination of many organic compounds, particularly proteins. EC
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.
Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.
A compound obtained from the bark of the white willow and wintergreen leaves. It has bacteriostatic, fungicidal, and keratolytic actions.
Very young plant after GERMINATION of SEEDS.
The synthesis by organisms of organic chemical compounds, especially carbohydrates, from carbon dioxide using energy obtained from light rather than from the oxidation of chemical compounds. Photosynthesis comprises two separate processes: the light reactions and the dark reactions. In higher plants; GREEN ALGAE; and CYANOBACTERIA; NADPH and ATP formed by the light reactions drive the dark reactions which result in the fixation of carbon dioxide. (from Oxford Dictionary of Biochemistry and Molecular Biology, 2001)
The large family of plants characterized by pods. Some are edible and some cause LATHYRISM or FAVISM and other forms of poisoning. Other species yield useful materials like gums from ACACIA and various LECTINS like PHYTOHEMAGGLUTININS from PHASEOLUS. Many of them harbor NITROGEN FIXATION bacteria on their roots. Many but not all species of "beans" belong to this family.
Porphyrin derivatives containing magnesium that act to convert light energy in photosynthetic organisms.
Microbodies which occur in animal and plant cells and in certain fungi and protozoa. They contain peroxidase, catalase, and allied enzymes. (From Singleton and Sainsbury, Dictionary of Microbiology and Molecular Biology, 2nd ed)
PLANTS, or their progeny, whose GENOME has been altered by GENETIC ENGINEERING.
Plants or plant parts which are harmful to man or other animals.
The usually underground portions of a plant that serve as support, store food, and through which water and mineral nutrients enter the plant. (From American Heritage Dictionary, 1982; Concise Dictionary of Biology, 1990)
Abscission-accelerating plant growth substance isolated from young cotton fruit, leaves of sycamore, birch, and other plants, and from potatoes, lemons, avocados, and other fruits.
Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.
Membranous cisternae of the CHLOROPLAST containing photosynthetic pigments, reaction centers, and the electron-transport chain. Each thylakoid consists of a flattened sac of membrane enclosing a narrow intra-thylakoid space (Lackie and Dow, Dictionary of Cell Biology, 2nd ed). Individual thylakoids are interconnected and tend to stack to form aggregates called grana. They are found in cyanobacteria and all plants.
The functional hereditary units of PLANTS.
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.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A poisonous dipyridilium compound used as contact herbicide. Contact with concentrated solutions causes irritation of the skin, cracking and shedding of the nails, and delayed healing of cuts and wounds.
Plants whose roots, leaves, seeds, bark, or other constituent parts possess therapeutic, tonic, purgative, curative or other pharmacologic attributes, when administered to man or animals.
Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor.
An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS.
Knobbed structures formed from and attached to plant roots, especially of LEGUMES, which result from symbiotic infection by nitrogen fixing bacteria such as RHIZOBIUM or FRANKIA. Root nodules are structures related to MYCORRHIZAE formed by symbiotic associations with fungi.
The unfavorable effect of environmental factors (stressors) on the physiological functions of an organism. Prolonged unresolved physiological stress can affect HOMEOSTASIS of the organism, and may lead to damaging or pathological conditions.
The rate dynamics in chemical or physical systems.
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.

In vivo role of catalase-peroxidase in synechocystis sp. strain PCC 6803. (1/206)

The katG gene coding for the only catalase-peroxidase in the cyanobacterium Synechocystis sp. strain PCC 6803 was deleted in this organism. Although the rate of H2O2 decomposition was about 30 times lower in the DeltakatG mutant than in the wild type, the strain had a normal phenotype and its doubling time as well as its resistance to H2O2 and methyl viologen were indistinguishable from those of the wild type. The residual H2O2-scavenging capacity was more than sufficient to deal with the rate of H2O2 production by the cell, estimated to be less than 1% of the maximum rate of photosynthetic electron transport in vivo. We propose that catalase-peroxidase has a protective role against environmental H2O2 generated by algae or bacteria in the ecosystem (for example, in mats). This protective role is most apparent at a high cell density of the cyanobacterium. The residual H2O2-scavenging activity in the DeltakatG mutant was a light-dependent peroxidase activity. However, neither glutathione peroxidase nor ascorbate peroxidase accounted for a significant part of this H2O2-scavenging activity. When a small thiol such as dithiothreitol was added to the medium, the rate of H2O2 decomposition in the DeltakatG mutant increased more than 10-fold, indicating that a thiol-specific peroxidase, for which thioredoxin may be the physiological electron donor, is present. Oxidized thioredoxin is likely to be reduced again by photosynthetic electron transport. Therefore, under laboratory conditions, there are only two enzymatic mechanisms for H2O2 decomposition present in Synechocystis sp. strain PCC 6803. One is catalyzed by a catalase-peroxidase, and the other is catalyzed by thiol-specific peroxidase.  (+info)

Systemic signaling and acclimation in response to excess excitation energy in Arabidopsis. (2/206)

Land plants are sessile and have developed sophisticated mechanisms that allow for both immediate and acclimatory responses to changing environments. Partial exposure of low light-adapted Arabidopsis plants to excess light results in a systemic acclimation to excess excitation energy and consequent photooxidative stress in unexposed leaves. Thus, plants possess a mechanism to communicate excess excitation energy systemically, allowing them to mount a defense against further episodes of such stress. Systemic redox changes in the proximity of photosystem II, hydrogen peroxide, and the induction of antioxidant defenses are key determinants of this mechanism of systemic acquired acclimation.  (+info)

Induction of ascorbate peroxidase by ethylene and hydrogen peroxide during growth of cultured soybean cells. (3/206)

In cultured soybean cells, a transient ethylene burst in the pre-stationary phase was followed by an induction of ascorbate peroxidase (AsPOX) in the stationary phase. Treatment of cells with the ethylene antagonist, silver thiosulfate (STS), resulted in the suppression of enzyme activity. Application of the ethylene releasing agent 2-chloroethylphosphonic acid (CEPA) in the medium led to an increased enzyme activity when treated in the pre-stationary phase. On the contrary, a remarkable inhibitory effect on enzyme activity was elicited by 1,3-dimethyl-2-thiourea (DMTU), trapping the hydrogen peroxide generated when treated in the stationary phase. Likewise, a steady level of AsPOX transcript was reduced by STS treatment. Furthermore, its effect appeared to be more rapid and prominent during the pre-stationary phase. It is suggested that the induction of AsPOX in cultured soybean cells during the stationary phase could result, at least in part, by the hydrogen peroxide generated as a result of preceding ethylene production.  (+info)

Stress-induced legume root nodule senescence. Physiological, biochemical, and structural alterations. (4/206)

Nitrate-fed and dark-stressed bean (Phaseolus vulgaris) and pea (Pisum sativum) plants were used to study nodule senescence. In bean, 1 d of nitrate treatment caused a partially reversible decline in nitrogenase activity and an increase in O(2) diffusion resistance, but minimal changes in carbon metabolites, antioxidants, and other biochemical parameters, indicating that the initial decrease in nitrogenase activity was due to O(2) limitation. In pea, 1 d of dark treatment led to a 96% decline in nitrogenase activity and sucrose, indicating sugar deprivation as the primary cause of activity loss. In later stages of senescence (4 d of nitrate or 2-4 d of dark treatment), nodules showed accumulation of oxidized proteins and general ultrastructural deterioration. The major thiol tripeptides of untreated nodules were homoglutathione (72%) in bean and glutathione (89%) in pea. These predominant thiols declined by approximately 93% after 4 d of nitrate or dark treatment, but the loss of thiol content can be only ascribed in part to limited synthesis by gamma-glutamylcysteinyl, homoglutathione, and glutathione synthetases. Ascorbate peroxidase was immunolocalized primarily in the infected and parenchyma (inner cortex) nodule cells, with large decreases in senescent tissue. Ferritin was almost undetectable in untreated bean nodules, but accumulated in the plastids and amyloplasts of uninfected interstitial and parenchyma cells following 2 or 4 d of nitrate treatment, probably as a response to oxidative stress.  (+info)

Peroxisomal membrane ascorbate peroxidase is sorted to a membranous network that resembles a subdomain of the endoplasmic reticulum. (5/206)

The peroxisomal isoform of ascorbate peroxidase (APX) is a novel membrane isoform that functions in the regeneration of NAD(+) and protection against toxic reactive oxygen species. The intracellular localization and sorting of peroxisomal APX were examined both in vivo and in vitro. Epitope-tagged peroxisomal APX, which was expressed transiently in tobacco BY-2 cells, localized to a reticular/circular network that resembled endoplasmic reticulum (ER; 3,3'-dihexyloxacarbocyanine iodide-stained membranes) and to peroxisomes. The reticular network did not colocalize with other organelle marker proteins, including three ER reticuloplasmins. However, in vitro, peroxisomal APX inserted post-translationally into the ER but not into other purified organelle membranes (including peroxisomal membranes). Insertion into the ER depended on the presence of molecular chaperones and ATP. These results suggest that regions of the ER serve as a possible intermediate in the sorting pathway of peroxisomal APX. Insight into this hypothesis was obtained from in vivo experiments with brefeldin A (BFA), a toxin that blocks vesicle-mediated protein export from ER. A transiently expressed chloramphenicol acetyltransferase-peroxisomal APX (CAT-pAPX) fusion protein accumulated only in the reticular/circular network in BFA-treated cells; after subsequent removal of BFA from these cells, the CAT-pAPX was distributed to preexisting peroxisomes. Thus, plant peroxisomal APX, a representative enzymatic peroxisomal membrane protein, is sorted to peroxisomes through an indirect pathway involving a preperoxisomal compartment with characteristics of a distinct subdomain of the ER, possibly a peroxisomal ER subdomain.  (+info)

Transgenic tobacco plants with reduced capability to detoxify reactive oxygen intermediates are hyperresponsive to pathogen infection. (6/206)

Reactive oxygen intermediates (ROI) play a critical role in the defense of plants against invading pathogens. Produced during the "oxidative burst," they are thought to activate programmed cell death (PCD) and induce antimicrobial defenses such as pathogenesis-related proteins. It was shown recently that during the interaction of plants with pathogens, the expression of ROI-detoxifying enzymes such as ascorbate peroxidase (APX) and catalase (CAT) is suppressed. It was suggested that this suppression, occurring upon pathogen recognition and coinciding with an enhanced rate of ROI production, plays a key role in elevating cellular ROI levels, thereby potentiating the induction of PCD and other defenses. To examine the relationship between the suppression of antioxidative mechanisms and the induction of PCD and other defenses during pathogen attack, we studied the interaction between transgenic antisense tobacco plants with reduced APX or CAT and a bacterial pathogen that triggers the hypersensitive response. Transgenic plants with reduced capability to detoxify ROI (i.e., antisense APX or CAT) were found to be hyperresponsive to pathogen attack. They activated PCD in response to low amounts of pathogens that did not trigger the activation of PCD in control plants. Our findings support the hypothesis that suppression of ROI-scavenging enzymes during the hypersensitive response plays an important role in enhancing pathogen-induced PCD.  (+info)

Chlororespiration and poising of cyclic electron transport. Plastoquinone as electron transporter between thylakoid NADH dehydrogenase and peroxidase. (7/206)

Polypeptides encoded by plastid ndh genes form a complex (Ndh) which could reduce plastoquinone with NADH. Through a terminal oxidase, reduced plastoquinone would be oxidized in chlororespiration. However, isolated Ndh complex has low activity with plastoquinone and no terminal oxidase has been found in chloroplasts, thus the function of Ndh complex is unknown. Alternatively, thylakoid hydroquinone peroxidase could oxidize reduced plastoquinone with H(2)O(2). By immunoaffinity chromatography, we have purified the plastid Ndh complex of barley (Hordeum vulgare L.) to investigate the electron donor and acceptor specificity. A detergent-containing system was reconstructed with thylakoid Ndh complex and peroxidase which oxidized NADH with H(2)O(2) in a plastoquinone-dependent process. This system and the increases of thylakoid Ndh complex and peroxidase activities under photooxidative stress suggest that the chlororespiratory process consists of the sequence of reactions catalyzed by Ndh complex, peroxidase (acting on reduced plastoquinone), superoxide dismutase, and the non-enzymic one-electron transfer from reduced iron-sulfur protein (FeSP) to O(2). When FeSP is a component of cytochrome b(6).f complex or of the same Ndh complex, O(2) may be reduced with NADH, without requirement of light. Chlororespiration consumes reactive species of oxygen and, eventually, may decrease their production by lowering O(2) concentration in chloroplasts. The common plastoquinone pool with photosynthetic electron transport suggests that chlororespiratory reactions may poise reduced and oxidized forms of the intermediates of cyclic electron transport under highly fluctuating light intensities.  (+info)

The sorting signals for peroxisomal membrane-bound ascorbate peroxidase are within its C-terminal tail. (8/206)

Peroxisomal ascorbate peroxidase (APX) is a carboxyl tail-anchored, type II (N(cytosol)-C(matrix)) integral membrane protein that functions in the regeneration of NAD(+) in glyoxysomes of germinated oilseeds and protection of peroxisomes in other organisms from toxic H(2)O(2). Recently we showed that cottonseed peroxisomal APX was sorted post-translationally from the cytosol to peroxisomes via a novel reticular/circular membranous network that was interpreted to be a subdomain of the endoplasmic reticulum (ER), named peroxisomal ER (pER). Here we report on the molecular signals responsible for sorting peroxisomal APX. Deletions or site-specific substitutions of certain amino acid residues within the hydrophilic C-terminal-most eight-amino acid residues (includes a positively charged domain found in most peroxisomal integral membrane-destined proteins) abolished sorting of peroxisomal APX to peroxisomes via pER. However, the C-terminal tail was not sufficient for sorting chloramphenicol acetyltransferase to peroxisomes via pER, whereas the peptide plus most of the immediately adjacent 21-amino acid transmembrane domain (TMD) of peroxisomal APX was sufficient for sorting. Replacement of the peroxisomal APX TMD with an artificial TMD (devoid of putative sorting sequences) plus the peroxisomal APX C-terminal tail also sorted chloramphenicol acetyltransferase to peroxisomes via pER, indicating that the peroxisomal APX TMD does not possess essential sorting information. Instead, the TMD appears to confer the proper context required for the conserved positively charged domain to function within peroxisomal APX as an overlapping pER sorting signal and a membrane peroxisome targeting signal type 2.  (+info)

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

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

Ascorbate oxidase is an enzyme that catalyzes the oxidation of ascorbic acid (vitamin C) to dehydroascorbic acid in the presence of oxygen. This reaction also results in the production of water and hydrogen peroxide as byproducts. Ascorbate oxidase plays a significant role in regulating the levels of ascorbic acid in plants, where it is primarily found. It belongs to the family of copper-containing oxidoreductases. The enzyme's active site contains two copper ions that facilitate the electron transfer during the catalytic process. Ascorbate oxidase is not considered essential for human health since humans do not produce ascorbic acid and must obtain it through dietary sources.

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

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

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

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

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

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

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

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

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

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

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

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

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.

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

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

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

H2O2 + 2e- + 2H+ → 2H2O

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

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

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

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

H2O2 + Catalase → H2O + O2 + Catalase

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

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

Chloroplasts are organelles found in the cells of plants, algae, and some protists. They are responsible for carrying out photosynthesis, which is the process by which these organisms convert light energy into chemical energy. Chloroplast proteins are the various proteins that are located within the chloroplasts and play a crucial role in the process of photosynthesis.

Chloroplasts contain several types of proteins, including:

1. Structural proteins: These proteins help to maintain the structure and integrity of the chloroplast.
2. Photosynthetic proteins: These are involved in capturing light energy and converting it into chemical energy during photosynthesis. They include proteins such as photosystem I, photosystem II, cytochrome b6f complex, and ATP synthase.
3. Regulatory proteins: These proteins help to regulate the various processes that occur within the chloroplast, including gene expression, protein synthesis, and energy metabolism.
4. Metabolic proteins: These proteins are involved in various metabolic pathways within the chloroplast, such as carbon fixation, amino acid synthesis, and lipid metabolism.
5. Protective proteins: These proteins help to protect the chloroplast from damage caused by reactive oxygen species (ROS) that are produced during photosynthesis.

Overall, chloroplast proteins play a critical role in maintaining the health and function of chloroplasts, and by extension, the overall health and survival of plants and other organisms that contain them.

Chloroplasts are specialized organelles found in the cells of green plants, algae, and some protists. They are responsible for carrying out photosynthesis, which is the process by which these organisms convert light energy from the sun into chemical energy in the form of organic compounds, such as glucose.

Chloroplasts contain the pigment chlorophyll, which absorbs light energy from the sun. They also contain a system of membranes and enzymes that convert carbon dioxide and water into glucose and oxygen through a series of chemical reactions known as the Calvin cycle. This process not only provides energy for the organism but also releases oxygen as a byproduct, which is essential for the survival of most life forms on Earth.

Chloroplasts are believed to have originated from ancient cyanobacteria that were engulfed by early eukaryotic cells and eventually became integrated into their host's cellular machinery through a process called endosymbiosis. Over time, chloroplasts evolved to become an essential component of plant and algal cells, contributing to their ability to carry out photosynthesis and thrive in a wide range of environments.

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.

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

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

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

Gene expression regulation in plants refers to the processes that control the production of proteins and RNA from the genes present in the plant's DNA. This regulation is crucial for normal growth, development, and response to environmental stimuli in plants. It can occur at various levels, including transcription (the first step in gene expression, where the DNA sequence is copied into RNA), RNA processing (such as alternative splicing, which generates different mRNA molecules from a single gene), translation (where the information in the mRNA is used to produce a protein), and post-translational modification (where proteins are chemically modified after they have been synthesized).

In plants, gene expression regulation can be influenced by various factors such as hormones, light, temperature, and stress. Plants use complex networks of transcription factors, chromatin remodeling complexes, and small RNAs to regulate gene expression in response to these signals. Understanding the mechanisms of gene expression regulation in plants is important for basic research, as well as for developing crops with improved traits such as increased yield, stress tolerance, and disease resistance.

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

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

"Spinacia oleracea" is the scientific name for a plant species, not a medical term. It is commonly known as spinach, a leafy green vegetable. While spinach has many health benefits and is often recommended as part of a balanced diet, it does not have a specific medical definition.

Spinach is rich in various nutrients such as iron, calcium, vitamin A, vitamin C, and folic acid. It can contribute to overall health, support immune function, and provide antioxidant benefits. However, it is important to note that 'Spinacia oleracea' itself does not have a medical definition.

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.

I'm sorry for any confusion, but "peas" is not a term typically used in medical definitions. Peas are a type of legume that is commonly consumed as a vegetable. They are rich in nutrients such as protein, fiber, vitamin C, and vitamin K. If you have any questions about the health benefits or potential risks of consuming peas, I would be happy to try to help with that.

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

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

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

Medical Definition:

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

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

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

'Arabidopsis' is a genus of small flowering plants that are part of the mustard family (Brassicaceae). The most commonly studied species within this genus is 'Arabidopsis thaliana', which is often used as a model organism in plant biology and genetics research. This plant is native to Eurasia and Africa, and it has a small genome that has been fully sequenced. It is known for its short life cycle, self-fertilization, and ease of growth, making it an ideal subject for studying various aspects of plant biology, including development, metabolism, and response to environmental stresses.

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.

Cytosol refers to the liquid portion of the cytoplasm found within a eukaryotic cell, excluding the organelles and structures suspended in it. It is the site of various metabolic activities and contains a variety of ions, small molecules, and enzymes. The cytosol is where many biochemical reactions take place, including glycolysis, protein synthesis, and the regulation of cellular pH. It is also where some organelles, such as ribosomes and vesicles, are located. In contrast to the cytosol, the term "cytoplasm" refers to the entire contents of a cell, including both the cytosol and the organelles suspended within it.

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

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

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

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

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

Dehydroascorbic acid (DHAA) is the oxidized form of ascorbic acid, which is more commonly known as vitamin C. It is the oxidation product of ascorbic acid that is formed when the vitamin C molecule loses two electrons and two protons. This conversion can occur naturally in the body or during the processing and storage of food.

DHAA still retains some vitamin C activity, but it is not as biologically active as ascorbic acid. However, DHAA can be reduced back to ascorbic acid in the body by certain enzymes, which allows it to still contribute to maintaining proper levels of this essential nutrient.

DHAA plays a role in various physiological processes, including collagen synthesis, immune function, and antioxidant defense. It is also involved in the metabolism of amino acids, carbohydrates, and lipids. A deficiency in vitamin C can lead to scurvy, a condition characterized by fatigue, joint pain, anemia, and skin changes.

"Drought" is not a medical term. It is a term used in meteorology and environmental science to refer to a prolonged period of abnormally low rainfall, leading to water shortage and scarcity in the affected areas. Droughts can have various impacts on human health, including dehydration, heat-related illnesses, reduced air quality, increased transmission of waterborne diseases, and mental health issues related to stress and displacement. However, drought itself is not a medical condition.

Tobacco is not a medical term, but it refers to the leaves of the plant Nicotiana tabacum that are dried and fermented before being used in a variety of ways. Medically speaking, tobacco is often referred to in the context of its health effects. According to the World Health Organization (WHO), "tobacco" can also refer to any product prepared from the leaf of the tobacco plant for smoking, sucking, chewing or snuffing.

Tobacco use is a major risk factor for a number of diseases, including cancer, heart disease, stroke, lung disease, and various other medical conditions. The smoke produced by burning tobacco contains thousands of chemicals, many of which are toxic and can cause serious health problems. Nicotine, one of the primary active constituents in tobacco, is highly addictive and can lead to dependence.

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

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

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

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.

Arabidopsis proteins refer to the proteins that are encoded by the genes in the Arabidopsis thaliana plant, which is a model organism commonly used in plant biology research. This small flowering plant has a compact genome and a short life cycle, making it an ideal subject for studying various biological processes in plants.

Arabidopsis proteins play crucial roles in many cellular functions, such as metabolism, signaling, regulation of gene expression, response to environmental stresses, and developmental processes. Research on Arabidopsis proteins has contributed significantly to our understanding of plant biology and has provided valuable insights into the molecular mechanisms underlying various agronomic traits.

Some examples of Arabidopsis proteins include transcription factors, kinases, phosphatases, receptors, enzymes, and structural proteins. These proteins can be studied using a variety of techniques, such as biochemical assays, protein-protein interaction studies, and genetic approaches, to understand their functions and regulatory mechanisms in plants.

Salicylic Acid is a type of beta hydroxy acid (BHA) that is commonly used in dermatology due to its keratolytic and anti-inflammatory properties. It works by causing the cells of the epidermis to shed more easily, preventing the pores from becoming blocked and promoting the growth of new skin cells. Salicylic Acid is also a potent anti-inflammatory agent, which makes it useful in the treatment of inflammatory acne and other skin conditions associated with redness and irritation. It can be found in various over-the-counter skincare products, such as cleansers, creams, and peels, as well as in prescription-strength formulations.

I'm sorry for any confusion, but "seedling" is not a term that has a specific medical definition. It is an agricultural and horticultural term that refers to a young plant grown from a seed, typically during the early stages of its growth. If you have any questions related to health or medicine, I'd be happy to try to help with those!

Photosynthesis is not strictly a medical term, but it is a fundamental biological process with significant implications for medicine, particularly in understanding energy production in cells and the role of oxygen in sustaining life. Here's a general biological definition:

Photosynthesis is a process by which plants, algae, and some bacteria convert light energy, usually from the sun, into chemical energy in the form of organic compounds, such as glucose (or sugar), using water and carbon dioxide. This process primarily takes place in the chloroplasts of plant cells, specifically in structures called thylakoids. The overall reaction can be summarized as:

6 CO2 + 6 H2O + light energy → C6H12O6 + 6 O2

In this equation, carbon dioxide (CO2) and water (H2O) are the reactants, while glucose (C6H12O6) and oxygen (O2) are the products. Photosynthesis has two main stages: the light-dependent reactions and the light-independent reactions (Calvin cycle). The light-dependent reactions occur in the thylakoid membrane and involve the conversion of light energy into ATP and NADPH, which are used to power the Calvin cycle. The Calvin cycle takes place in the stroma of chloroplasts and involves the synthesis of glucose from CO2 and water using the ATP and NADPH generated during the light-dependent reactions.

Understanding photosynthesis is crucial for understanding various biological processes, including cellular respiration, plant metabolism, and the global carbon cycle. Additionally, research into artificial photosynthesis has potential applications in renewable energy production and environmental remediation.

Fabaceae is the scientific name for a family of flowering plants commonly known as the legume, pea, or bean family. This family includes a wide variety of plants that are important economically, agriculturally, and ecologically. Many members of Fabaceae have compound leaves and produce fruits that are legumes, which are long, thin pods that contain seeds. Some well-known examples of plants in this family include beans, peas, lentils, peanuts, clover, and alfalfa.

In addition to their importance as food crops, many Fabaceae species have the ability to fix nitrogen from the atmosphere into the soil through a symbiotic relationship with bacteria that live in nodules on their roots. This makes them valuable for improving soil fertility and is one reason why they are often used in crop rotation and as cover crops.

It's worth noting that Fabaceae is sometimes still referred to by its older scientific name, Leguminosae.

Chlorophyll is a green pigment found in the chloroplasts of photosynthetic plants, algae, and some bacteria. It plays an essential role in light-dependent reactions of photosynthesis by absorbing light energy, primarily from the blue and red parts of the electromagnetic spectrum, and converting it into chemical energy to fuel the synthesis of carbohydrates from carbon dioxide and water. The structure of chlorophyll includes a porphyrin ring, which binds a central magnesium ion, and a long phytol tail. There are several types of chlorophyll, including chlorophyll a and chlorophyll b, which have distinct absorption spectra and slightly different structures. Chlorophyll is crucial for the process of photosynthesis, enabling the conversion of sunlight into chemical energy and the release of oxygen as a byproduct.

Peroxisomes are membrane-bound subcellular organelles found in the cytoplasm of eukaryotic cells. They play a crucial role in various cellular processes, including the breakdown of fatty acids and the detoxification of harmful substances such as hydrogen peroxide (H2O2). Peroxisomes contain numerous enzymes, including catalase, which converts H2O2 into water and oxygen, thus preventing oxidative damage to cellular components. They also participate in the biosynthesis of ether phospholipids, a type of lipid essential for the structure and function of cell membranes. Additionally, peroxisomes are involved in the metabolism of reactive oxygen species (ROS) and contribute to the regulation of intracellular redox homeostasis. Dysfunction or impairment of peroxisome function has been linked to several diseases, including neurological disorders, developmental abnormalities, and metabolic conditions.

Genetically modified plants (GMPs) are plants that have had their DNA altered through genetic engineering techniques to exhibit desired traits. These modifications can be made to enhance certain characteristics such as increased resistance to pests, improved tolerance to environmental stresses like drought or salinity, or enhanced nutritional content. The process often involves introducing genes from other organisms, such as bacteria or viruses, into the plant's genome. Examples of GMPs include Bt cotton, which has a gene from the bacterium Bacillus thuringiensis that makes it resistant to certain pests, and golden rice, which is engineered to contain higher levels of beta-carotene, a precursor to vitamin A. It's important to note that genetically modified plants are subject to rigorous testing and regulation to ensure their safety for human consumption and environmental impact before they are approved for commercial use.

'Toxic plants' refer to those species of plants that contain toxic substances capable of causing harmful effects or adverse health reactions in humans and animals when ingested, touched, or inhaled. These toxins can cause a range of symptoms from mild irritation to serious conditions such as organ failure, paralysis, or even death depending on the plant, the amount consumed, and the individual's sensitivity to the toxin.

Toxic plants may contain various types of toxins, including alkaloids, glycosides, proteins, resinous substances, and essential oils. Some common examples of toxic plants include poison ivy, poison oak, nightshade, hemlock, oleander, castor bean, and foxglove. It is important to note that some parts of a plant may be toxic while others are not, and the toxicity can also vary depending on the stage of growth or environmental conditions.

If you suspect exposure to a toxic plant, it is essential to seek medical attention immediately and, if possible, bring a sample of the plant for identification.

A plant root is not a medical term per se, but it is a term from botany, which is the study of plants. However, I can certainly provide a definition for you.

Plant roots are the underground organs of a plant that typically grow downward into the soil. They serve several important functions, including:

1. Anchorage: Roots help to stabilize the plant and keep it upright in the ground.
2. Absorption: Roots absorb water and nutrients from the soil, which are essential for the plant's growth and development.
3. Conduction: Roots conduct water and nutrients up to the above-ground parts of the plant, such as the stem and leaves.
4. Vegetative reproduction: Some plants can reproduce vegetatively through their roots, producing new plants from root fragments or specialized structures called rhizomes or tubers.

Roots are composed of several different tissues, including the epidermis, cortex, endodermis, and vascular tissue. The epidermis is the outermost layer of the root, which secretes a waxy substance called suberin that helps to prevent water loss. The cortex is the middle layer of the root, which contains cells that store carbohydrates and other nutrients. The endodermis is a thin layer of cells that surrounds the vascular tissue and regulates the movement of water and solutes into and out of the root. The vascular tissue consists of xylem and phloem, which transport water and nutrients throughout the plant.

Abscisic acid (ABA) is a plant hormone that plays a crucial role in the regulation of various physiological processes, including seed dormancy, bud dormancy, leaf senescence, and response to abiotic stresses such as drought, salinity, and cold temperatures. It is a sesquiterpene compound that is synthesized in plants primarily in response to environmental stimuli that trigger the onset of stress responses.

ABA functions by regulating gene expression, cell growth and development, and stomatal closure, which helps prevent water loss from plants under drought conditions. It also plays a role in the regulation of plant metabolism and the activation of defense mechanisms against pathogens and other environmental stressors. Overall, abscisic acid is an essential hormone that enables plants to adapt to changing environmental conditions and optimize their growth and development.

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

Thylakoids are membrane-bound structures located in the chloroplasts of plant cells and some protists. They are the site of the light-dependent reactions of photosynthesis, where light energy is converted into chemical energy in the form of ATP (adenosine triphosphate) and NADPH (nicotinamide adenine dinucleotide phosphate). Thylakoids have a characteristic stacked or disc-like structure, called grana, and are interconnected by unstacked regions called stroma lamellae. The arrangement of thylakoids in grana increases the surface area for absorption of light energy, allowing for more efficient photosynthesis.

A gene in plants, like in other organisms, is a hereditary unit that carries genetic information from one generation to the next. It is a segment of DNA (deoxyribonucleic acid) that contains the instructions for the development and function of an organism. Genes in plants determine various traits such as flower color, plant height, resistance to diseases, and many others. They are responsible for encoding proteins and RNA molecules that play crucial roles in the growth, development, and reproduction of plants. Plant genes can be manipulated through traditional breeding methods or genetic engineering techniques to improve crop yield, enhance disease resistance, and increase nutritional value.

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.

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.

Paraquat is a highly toxic herbicide that is used for controlling weeds and grasses in agricultural settings. It is a non-selective contact weed killer, meaning it kills any green plant it comes into contact with. Paraquat is a fast-acting chemical that causes rapid desiccation of plant tissues upon contact.

In a medical context, paraquat is classified as a toxicological emergency and can cause severe poisoning in humans if ingested, inhaled, or comes into contact with the skin or eyes. Paraquat poisoning can lead to multiple organ failure, including the lungs, kidneys, and liver, and can be fatal in severe cases. There is no specific antidote for paraquat poisoning, and treatment typically focuses on supportive care and managing symptoms.

It's important to note that paraquat is highly regulated and its use is restricted to licensed professionals due to its high toxicity. Proper protective equipment, including gloves, goggles, and respiratory protection, should be used when handling paraquat to minimize the risk of exposure.

Medicinal plants are defined as those plants that contain naturally occurring chemical compounds which can be used for therapeutic purposes, either directly or indirectly. These plants have been used for centuries in various traditional systems of medicine, such as Ayurveda, Chinese medicine, and Native American medicine, to prevent or treat various health conditions.

Medicinal plants contain a wide variety of bioactive compounds, including alkaloids, flavonoids, tannins, terpenes, and saponins, among others. These compounds have been found to possess various pharmacological properties, such as anti-inflammatory, analgesic, antimicrobial, antioxidant, and anticancer activities.

Medicinal plants can be used in various forms, including whole plant material, extracts, essential oils, and isolated compounds. They can be administered through different routes, such as oral, topical, or respiratory, depending on the desired therapeutic effect.

It is important to note that while medicinal plants have been used safely and effectively for centuries, they should be used with caution and under the guidance of a healthcare professional. Some medicinal plants can interact with prescription medications or have adverse effects if used inappropriately.

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

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

I'm sorry for any confusion, but "soybeans" are not a medical term. They are a type of legume that is commonly used in agriculture and food production. The medical community might discuss soybeans in the context of nutrition or allergies, but there isn't a formal medical definition for this term.

Here's some general information: Soybeans, scientifically known as Glycine max, are native to East Asia and are now grown worldwide. They are a significant source of plant-based protein and oil. Soybeans contain various nutrients, including essential amino acids, fiber, B vitamins, and minerals like calcium, iron, magnesium, and zinc. They are used in various food products such as tofu, soy milk, tempeh, and miso. Additionally, soybeans are also used in the production of industrial products, including biodiesel, plastics, and inks. Some people may have allergic reactions to soybeans or soy products.

Root nodules in plants refer to the specialized structures formed through the symbiotic relationship between certain leguminous plants and nitrogen-fixing bacteria, most commonly belonging to the genus Rhizobia. These nodules typically develop on the roots of the host plant, providing an ideal environment for the bacteria to convert atmospheric nitrogen into ammonia, a form that can be directly utilized by the plant for growth and development.

The formation of root nodules begins with the infection of the plant's root hair cells by Rhizobia bacteria. This interaction triggers a series of molecular signals leading to the differentiation of root cortical cells into nodule primordia, which eventually develop into mature nodules. The nitrogen-fixing bacteria reside within these nodules in membrane-bound compartments called symbiosomes, where they reduce atmospheric nitrogen into ammonia through an enzyme called nitrogenase.

The plant, in turn, provides the bacteria with carbon sources and other essential nutrients required for their growth and survival within the nodules. The fixed nitrogen is then transported from the root nodules to other parts of the plant, enhancing its overall nitrogen nutrition and promoting sustainable growth without the need for external nitrogen fertilizers.

In summary, root nodules in plants are essential structures formed through symbiotic associations with nitrogen-fixing bacteria, allowing leguminous plants to convert atmospheric nitrogen into a usable form while also benefiting the environment by reducing the reliance on chemical nitrogen fertilizers.

Physiological stress is a response of the body to a demand or threat that disrupts homeostasis and activates the autonomic nervous system and hypothalamic-pituitary-adrenal (HPA) axis. This results in the release of stress hormones such as adrenaline, cortisol, and noradrenaline, which prepare the body for a "fight or flight" response. Increased heart rate, rapid breathing, heightened sensory perception, and increased alertness are some of the physiological changes that occur during this response. Chronic stress can have negative effects on various bodily functions, including the immune, cardiovascular, and nervous systems.

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.

In the context of medical terminology, "light" doesn't have a specific or standardized definition on its own. However, it can be used in various medical terms and phrases. For example, it could refer to:

1. Visible light: The range of electromagnetic radiation that can be detected by the human eye, typically between wavelengths of 400-700 nanometers. This is relevant in fields such as ophthalmology and optometry.
2. Therapeutic use of light: In some therapies, light is used to treat certain conditions. An example is phototherapy, which uses various wavelengths of ultraviolet (UV) or visible light for conditions like newborn jaundice, skin disorders, or seasonal affective disorder.
3. Light anesthesia: A state of reduced consciousness in which the patient remains responsive to verbal commands and physical stimulation. This is different from general anesthesia where the patient is completely unconscious.
4. Pain relief using light: Certain devices like transcutaneous electrical nerve stimulation (TENS) units have a 'light' setting, indicating lower intensity or frequency of electrical impulses used for pain management.

Without more context, it's hard to provide a precise medical definition of 'light'.

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

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

... ascorbate peroxidase, and ascorbic acid peroxidase. This enzyme participates in ascorbate and aldarate metabolism. Ascorbate- ... Ascorbate peroxidase (or L-ascorbate peroxidase, APX) (EC is an enzyme that catalyzes the chemical reaction L- ... Cytochrome c peroxidase Manganese peroxidase Kelly GJ, Latzko E (December 1979). "Soluble ascorbate peroxidase: detection in ... ascorbate peroxidases is a class I peroxidase enzyme. APXs catalyse the H2O2-dependent oxidation of ascorbate in plants, algae ...
"Substrate Binding and Catalytic Mechanism in Ascorbate Peroxidase: Evidence for Two Ascorbate Binding Sites †". Biochemistry. ... "Crystal structure of the ascorbate peroxidase-ascorbate complex". Nature Structural & Molecular Biology. 10 (4): 303-307. doi: ... "Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase" (PDF). Science. 345 (6193): 193-197 ...
H2O2 is reduced to water by ascorbate peroxidase (APX) using ascorbate (ASC) as the electron donor. The oxidized ascorbate ( ... Antioxidant Oxidative stress Peroxidases Noctor G, Foyer CH (Jun 1998). "ASCORBATE AND GLUTATHIONE: Keeping Active Oxygen Under ... Nevertheless, other enzymes (peroxidases) including peroxiredoxins and glutathione peroxidases, which use thioredoxins or ... ascorbate and NADPH are present in high concentrations in plant cells it is assumed that the glutathione-ascorbate cycle plays ...
"Characterization of ascorbate peroxidases from unicellular red alga Galdieria partita". Plant & Cell Physiology. 42 (4): 433- ...
CCP has high sequence identity to the closely related ascorbate peroxidase enzyme. Amino acid analyzer studies reveal presence ... Plant peroxidase such as horseradish peroxidase and pineapple peroxidase B have low lysine, tryptophan, and tyrosine contents ... Cytochrome c peroxidase, or CCP, is a water-soluble heme-containing enzyme of the peroxidase family that takes reducing ... Cytochrome c peroxidase, maintained by the Kraut Research Group. The UniProt entry for yeast cytochrome c peroxidase. Portal: ...
Both taxifolin and coniferyl alcohol will be oxidized by ascorbate peroxidase 1 to enable the single electron reaction to ... April 2019). "4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase". Nature ...
Martell, JD (2012). "Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy". Nature ... Martell, JD (2016). "A split horseradish peroxidase for the detection of intercellular protein-protein interactions and ... Paek, J (2017). "Multidimensional Tracking of GPCR Signaling via Peroxidase-Catalyzed Proximity Labeling". Cell. 169 (2): 338- ... the peroxidase APEX2, and the biotin ligases TurboID and miniTurbo. In addition, Ting and her lab developed monovalent ...
In UV-B exposed plants, the antioxidative enzymes superoxide dismutase, catalase, and peroxidase are synthesized. The exposed ... plants also synthesize the non-enzymatic antioxidants ascorbate, carotenoids, and flavonoids. All these antioxidants are also ...
... expression and functional validation of drought inducible ascorbate peroxidase (Ec-apx1) from Eleusine coracana". Molecular ...
M. mediterraneum helped chickpea resist osmotic stress by enhancing nodular peroxidase and ascorbate peroxidase activities. ...
Pal, Swati; Dolai, Subhankar; Yadav, Rajesh K.; Adak, Subrata (23 June 2010). "Ascorbate Peroxidase from Leishmania major ... Pal, Swati; Dolai, Subhankar; Yadav, Rajesh K.; Adak, Subrata (23 June 2010). "Ascorbate Peroxidase from Leishmania major ...
Dietz KJ (January 2016). "Thiol-Based Peroxidases and Ascorbate Peroxidases: Why Plants Rely on Multiple Peroxidase Systems in ... 2 H 2 O 2 → catalase 2 H 2 O + O 2 2 GSH + H 2 O 2 → glutathione peroxidase GS − SG + 2 H 2 O {\displaystyle {\begin{aligned ... Glutathione peroxidase reduces hydrogen peroxide by transferring the energy of the reactive peroxides to a sulfur-containing ... ascorbate) and β-carotene and anti-oxidant enzymes. If too much damage is present in mitochondria, a cell undergoes apoptosis ...
Ascorbate peroxidase Chloride peroxidase Cytochrome c peroxidase Haloperoxidase Hemoprotein Immunoperoxidase Lactoperoxidase ... Haem-using haem peroxidase and the related animal heme-dependent peroxidases DyP-type peroxidase family Catalase some ... Peroxidases are sometimes used as histological markers. Cytochrome c peroxidase is used as a soluble, easily purified model for ... Peroxidases typically catalyze a reaction of the form: ROOR ′ + 2 e − electron donor + 2 H + → Peroxidase ROH + R ′ OH {\ ...
... and ascorbate peroxidase (to scavenge hydrogen peroxide). After conducting his research on M. stellatus and C. crispus in 1999 ...
... ascorbate, carotenoids, superoxide dismutase, catalase, and glutathione peroxidase. These antioxidants provide protection from ...
... which is a signal to downregulate its own expression of ascorbate oxidase and ascorbate peroxidase. AO and AP are reactive ...
... ascorbate peroxidase, and glutathione peroxidase). The antioxidant superoxide dismutase catalyses the formation of hydrogen ... "Temporal mismatch between induction of superoxide dismutase and ascorbate peroxidase correlates with high H2O2 concentration in ...
One of these proximity labeling approaches is the ascorbate peroxidase (APEX) method, in which cells are engineered to express ... fused to a modified ascorbate peroxidase enzyme called APEX. Upon incubating the cells in biotin and treating the cells with ...
... a France anti-tank gun Ascorbate peroxidase, an antioxidant enzyme Lotus APX, a 2006 concept car Advanced Performance ...
... iodide peroxidase EC glutathione peroxidase EC chloride peroxidase EC L-ascorbate peroxidase EC ... NADH peroxidase EC NADPH peroxidase EC fatty-acid peroxidase EC Now EC EC ... versatile peroxidase EC glutathione amide-dependent peroxidase EC bromide peroxidase EC dye ... phospholipid-hydroperoxide glutathione peroxidase EC manganese peroxidase EC lignin peroxidase ...
It is a component of the glutathione-ascorbate cycle, a system that reduces poisonous hydrogen peroxide. It is the precursor of ... It is a cofactor and acts on glutathione peroxidase. Glutathione is used to produce S-sulfanylglutathione, which is part of ... Noctor G, Foyer CH (June 1998). "Ascorbate and Glutathione: Keeping Active Oxygen Under Control". Annual Review of Plant ... a tool to measure the cellular glutathione redox potential Glutathione-ascorbate cycle Bacterial glutathione transferase ...
In plants, vitamin C is a substrate for ascorbate peroxidase. This enzyme utilizes ascorbate to neutralize excess hydrogen ... Ascorbate salts such as sodium ascorbate and calcium ascorbate are used in some dietary supplements. These release ascorbate ... However, taking vitamin C in the form of sodium ascorbate and calcium ascorbate may minimize this effect. Other symptoms ... The most commonly used supplement compounds are ascorbic acid, sodium ascorbate and calcium ascorbate. Vitamin C molecules can ...
Glutathione-ascorbate cycle Antioxidant Meister A, Anderson ME (1983). "Glutathione". Annual Review of Biochemistry. 52: 711-60 ... Antioxidant enzymes, such as glutathione peroxidases and peroxiredoxins, generate glutathione disulfide during the reduction of ...
Monteiro G, Horta BB, Pimenta DC, Augusto O, Netto LE (March 2007). "Reduction of 1-Cys peroxiredoxins by ascorbate changes the ... Catalase Oxidative stress Peroxidase Peroxiredoxin classification index Reactive oxygen species Superoxide dismutase Rhee, Sue ... Other names include thiol specific antioxidant (TSA) and thioredoxin peroxidase (TPx). Mammals express six peroxiredoxins:. 1- ... Poole LB (January 2005). "Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their ...
... ascorbate, which is added to cured meat, however, reduces nitrosamine formation). Overly-browned starchy food such as bread, ... is a component of important antioxidant enzymes such as gluthathione peroxidase. Many phytonutrients may counter the effect of ...
For instance, glutathione peroxidases catalyze the oxidation of GSH to glutathione disulfide (GSSG) by reducing free radicals ... Jain A, Buist NR, Kennaway NG, Powell BR, Auld PA, Mårtensson J (Feb 1994). "Effect of ascorbate or N-acetylcysteine treatment ... After the final GSH product is made, it can be used by glutathione peroxidase to neutralize reactive oxygen species (ROS) such ... ascorbate and N-acetylcysteine have been shown to increase glutathione levels and increase erythrocyte production. It is ...
Reduced glutathione reduces the oxidized form of the enzyme glutathione peroxidase, which in turn reduces hydrogen peroxide ( ... In plants, reduced glutathione participates in the glutathione-ascorbate cycle in which reduced glutathione reduces ...
Sulfite may also be oxidized to sulfate, extra- and intracellularly by peroxidases or non-enzymatically catalyzed by metal ions ... Glutathione functions as reductant in the enzymatic detoxification of reactive oxygen species in the glutathione-ascorbate ...
Vegetable peroxidase and bacterial enzymes, including an Escherichia coli peroxidase, may also cause false-positive reactions. ... Some test strips include a test for urinary ascorbate. During routine screening, if a positive test for leukocytes, blood, ... The urine test strip test for blood is based on hemoglobin's pseudo peroxidase activity in catalysing a reaction between ... A second linked reaction, mediated by a peroxidase, catalyses the reaction between the peroxide and a chromogen (a substance ...
Dominguez, E.; Perez, M. D.; Calvo, M. (1997). "Effect of heat treatment on the antigen-binding activity of anti-peroxidase ... "Inhibition of Iron/Ascorbate-Induced Lipid Peroxidation by an N-Terminal Peptide of Bovine Lactoferrin and Its Acylated ...
doi:10.1016/0959-440X(92)90230-5. Dalton DA (1991). "Ascorbate peroxidase". 2: 139-153. {{cite journal}}: Cite journal requires ... peroxidases, exhibiting both peroxidase and catalase activities. It is thought that catalase-peroxidase provides protection to ... Haem peroxidases (or heme peroxidases) are haem-containing enzymes that use hydrogen peroxide as the electron acceptor to ... Another family of haem peroxidases is the DyP-type peroxidase family. Nelson RE, Fessler LI, Takagi Y, Blumberg B, Keene DR, ...
... such as ascorbate in the glutathione-ascorbate cycle, glutathione peroxidases and glutaredoxins, as well as reacting directly ... In addition to its direct antioxidant effects, ascorbic acid is also a substrate for the redox enzyme ascorbate peroxidase, a ... There are at least four different glutathione peroxidase isozymes in animals. Glutathione peroxidase 1 is the most abundant and ... "Regulation and function of ascorbate peroxidase isoenzymes". Journal of Experimental Botany. 53 (372): 1305-19. doi:10.1093/ ...
"Inactivation of Ascorbate Peroxidase in Spinach Chloroplasts on Dark Addition of Hydrogen Peroxide: Its Protection by Ascorbate ... "Monodehydroascorbate Reductase in Spinach Chloroplasts and Its Participation in Regeneration of Ascorbate for Scavenging ...
This photochemical H 2O 2 is then reduced by the action of ascorbate peroxidase to form water and oxidized ascorbate. Asada ...
APEX is an ascorbate peroxidase derivative reliant on hydrogen peroxide for catalyzing the oxidation of biotin-tyramide, also ... Kalocsay, Marian (2019). "APEX Peroxidase-Catalyzed Proximity Labeling and Multiplexed Quantitative Proteomics". In Sunbul, ... "Multidimensional Tracking of GPCR Signaling via Peroxidase-Catalyzed Proximity Labeling". Cell. 169 (2): 338-349.e11. doi: ...
Wefers H, Sies H (June 1988). "The protection by ascorbate and glutathione against microsomal lipid peroxidation is dependent ... Alpha-tocopherol is a lipid-soluble antioxidant functioning within the glutathione peroxidase pathway, and protecting cell ... such as ascorbate, retinol or ubiquinol. Other forms of vitamin E have their own unique properties; for example, γ-tocopherol ...
Electron donors may include ascorbate, cytochrome b5 or ferredoxin reductase. The catalytic NO dioxygenation can be written in ... and peroxidase. NODs, as well as many hemoglobins that function as NODs, are distributed to most life forms including bacteria ...

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