A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.
Materials that add an electron to an element or compound, that is, decrease the positiveness of its valence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.
Compounds containing the -SH radical.
Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
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).
Mercaptoethanol is a compound used in the treatment of certain genetic disorders, such as sickle cell anemia, by reducing the production of abnormal hemoglobin.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A sulfhydryl reagent that is widely used in experimental biochemical studies.
The rate dynamics in chemical or physical systems.
A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate.
A sulfhydryl reagent which oxidizes sulfhydryl groups to the disulfide form. It is a radiation-sensitizing agent of anoxic bacterial and mammalian cells.
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.
Benzoic acid esters or salts substituted with one or more iodine atoms.
Compounds which restore enzymatic activity by removing an inhibitory group bound to the reactive site of the enzyme.
The sum of the weight of all the atoms in a molecule.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
Chloride and mercury-containing derivatives of benzoic acid.
Hydroxylated benzoic acid derivatives that contain mercury. Some of these are used as sulfhydryl reagents in biochemical studies.
An ethylmercury-sulfidobenzoate that has been used as a preservative in VACCINES; ANTIVENINS; and OINTMENTS. It was formerly used as a topical antiseptic. It degrades to ethylmercury and thiosalicylate.
A compound that, along with its isomer, Cleland's reagent (DITHIOTHREITOL), is used for the protection of sulfhydryl groups against oxidation to disulfides and for the reduction of disulfides to sulfhydryl groups.
A chelating agent that sequesters a variety of polyvalent cations such as CALCIUM. It is used in pharmaceutical manufacturing and as a food additive.
A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
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 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.
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.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
An anti-gas warfare agent that is effective against Lewisite (dichloro(2-chlorovinyl)arsine) and formerly known as British Anti-Lewisite or BAL. It acts as a chelating agent and is used in the treatment of arsenic, gold, and other heavy metal poisoning.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
An organic mercurial used as a sulfhydryl reagent.
A sulfur-containing alkyl thionitrite that is one of the NITRIC OXIDE DONORS.
Electron-accepting molecules in chemical reactions in which electrons are transferred from one molecule to another (OXIDATION-REDUCTION).
A radiation-protective agent that interferes with sulfhydryl enzymes. It may also protect against carbon tetrachloride liver damage.
Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Inorganic derivatives of phosphorus trihydroxide (P(OH)3) and its tautomeric form dihydroxyphosphine oxide (HP=O(OH)2). Note that organic derivatives of phosphonic acids are listed under are ORGANOPHOSPHONATES.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Positively charged atoms, radicals or groups of atoms with a valence of plus 2, which travel to the cathode or negative pole during electrolysis.
Nitroso compounds are a class of chemicals that contain a nitroso group (-NO) and have various medical applications, including as vasodilators and as intermediates in the metabolism of drugs and toxins.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A subtype of thioredoxins found primarily in CHLOROPLASTS.
Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids.
The covalent bonding of an alkyl group to an organic compound. It can occur by a simple addition reaction or by substitution of another functional group.
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
A group of compounds that contain a bivalent O-O group, i.e., the oxygen atoms are univalent. They can either be inorganic or organic in nature. Such compounds release atomic (nascent) oxygen readily. Thus they are strong oxidizing agents and fire hazards when in contact with combustible materials, especially under high-temperature conditions. The chief industrial uses of peroxides are as oxidizing agents, bleaching agents, and initiators of polymerization. (From Hawley's Condensed Chemical Dictionary, 11th ed)
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
The extent to which an enzyme retains its structural conformation or its activity when subjected to storage, isolation, and purification or various other physical or chemical manipulations, including proteolytic enzymes and heat.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
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)
Proteins prepared by recombinant DNA technology.
A toxic thiol mercury salt formerly used as a diuretic. It inhibits various biochemical functions, especially in mitochondria, and is used to study those functions.
Purifying or cleansing agents, usually salts of long-chain aliphatic bases or acids, that exert cleansing (oil-dissolving) and antimicrobial effects through a surface action that depends on possessing both hydrophilic and hydrophobic properties.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
A diverse group of agents, with unique chemical structures and biochemical requirements, which generate NITRIC OXIDE. These compounds have been used in the treatment of cardiovascular diseases and the management of acute myocardial infarction, acute and chronic congestive heart failure, and surgical control of blood pressure. (Adv Pharmacol 1995;34:361-81)
The ability of a substance to be dissolved, i.e. to form a solution with another substance. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Peroxidases are enzymes that catalyze the oxidation of substrates by hydrogen peroxide or other peroxides, with applications in medical fields such as wound healing and cancer treatment.
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
The anterior portion of the spermatozoon (SPERMATOZOA) that contains mainly the nucleus with highly compact CHROMATIN material.
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.
A cytotoxic sulfhydryl reagent that inhibits several subcellular metabolic systems and is used as a tool in cellular physiology.

Regulation of 2-carboxy-D-arabinitol 1-phosphate phosphatase: activation by glutathione and interaction with thiol reagents. (1/2188)

2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase de- grades CA1P, an inhibitor associated with the regulation of ribulose bisphosphate carboxylase/oxygenase in numerous plant species. CA1P phosphatase purified from Phaseolus vulgaris was partially inactivated by oxidizing conditions during dialysis in air-equilibrated buffer. Phosphatase activity could then be stimulated 1.3-fold by dithiothreitol and also by addition of reduced thioredoxin from Escherichia coli. These effects were enhanced synergistically by the positive effector, fructose 1, 6-bisphosphate (FBP). Most notably, CA1P phosphatase activity was stimulated up to 35-fold by glutathione, and was sensitive to the ratio of reduced (GSH) to oxidized (GSSG) forms. At concentrations of glutathione approximating measured levels in chloroplasts of P. vulgaris (5 mM total S), CA1P phosphatase exhibited >20-fold stimulation by a change in the redox status of glutathione from 60 to 100% GSH. This stimulation was augmented further by reduced E. coli thioredoxin. In contrast, FBP, which activates CA1P phosphatase under reducing conditions, was strongly inhibitory in the presence of GSSG. We propose that glutathione may have an appreciable role in the light/dark regulation of CA1P phosphatase in vivo. A model for the reversible activation of CA1P phosphatase by GSH was derived based upon the various responses of the enzyme's activity to a range of thiol reagents including N-ethylmaleimide, 5, 5'-dithiobis-(2-nitrobenzoic acid) and arsenite. These data indicate that the bean enzyme contains two physically distinct sets of thiol groups that are critical to its redox regulation.  (+info)

In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli. (2/2188)

We have found that the in vivo folding of periplasmic Escherichia coli Cu,Zn superoxide dismutase is assisted by DsbA, which catalyzes the efficient formation of its single disulfide bond, whose integrity is essential to ensure full catalytic activity to the enzyme. In line with these findings, we also report that the production of recombinant Xenopus laevis Cu,Zn superoxide dismutase is enhanced when the enzyme is exported in the periplasmic space or is expressed in thioredoxin reductase mutant strains. Our data show that inefficient disulfide bond oxidation in the bacterial cytoplasm inhibits Cu,Zn superoxide dismutase folding in this cellular compartment.  (+info)

An intact sperm nuclear matrix may be necessary for the mouse paternal genome to participate in embryonic development. (3/2188)

We have been interested in determining the minimally required elements in the sperm head that are necessary in order for the paternal genome to participate in embryogenesis. We used an ionic detergent, mixed alkyltrimethylammonium bromide (ATAB), plus dithiothreitol (DTT) to remove the acrosome and almost all of the perinuclear theca, leaving only the sperm nucleus morphologically intact. We also tested the stability of the sperm nuclear matrix by the ability to form nuclear halos. Sperm nuclei washed in freshly prepared 0.5% ATAB + 2 mM DTT completely decondensed when extracted with salt, but nuclei washed in the same buffer that was 1 wk old, and then extracted with salt, produced nuclear halos, indicating stable nuclear matrices. When we treated sperm heads with freshly prepared ATAB+DTT and injected them into oocytes, none of the oocytes developed into live offspring. In contrast, sperm heads treated in the same way but with 1-wk-old ATAB+DTT solution could support development of about 30% of the oocytes to live offspring. Electron microscopy demonstrated that most of the perinuclear theca had been removed in both cases. These data suggest that at least in the mouse, the only component of the spermatozoa that is crucial for participation in embryologic development is the sperm nucleus with a stable nuclear matrix.  (+info)

A novel trans-complementation assay suggests full mammalian oocyte activation is coordinately initiated by multiple, submembrane sperm components. (4/2188)

To initiate normal embryonic development, an egg must receive a signal to become activated at fertilization. We here report that the ability of demembranated sperm heads to activate is abolished after incubation over the range 20-44 degreesC and is sensitive to reducing agents. On the basis of this observation, we have developed a microinjection-based, trans-complementation assay in order to dissect the heat-inactivated sperm-borne oocyte-activating factor(s) (SOAF). We demonstrate that the failure of heat-inactivated sperm heads to activate an egg is rescued by coinjection with dithiothreitol-solubilized SOAF from demembranated sperm heads. The solubilized SOAF (SOAFs) is trypsin sensitive and is liberated from demembranated heads in a temperature-dependent manner that inversely correlates with the ability of sperm heads to activate. This argues that SOAFs is a proteinaceous molecular species required to initiate activation. Injection of oocytes with mouse or hamster sperm cytosolic factors, but not SOAFs alone, induced resumption of meiosis, further suggesting that these cytosolic factors and SOAF are distinct. Collectively, these data strongly suggest that full mammalian oocyte activation is initiated by the coordinated action of one or more heat-sensitive protein constituents of the perinuclear matrix and at least one heat-stable submembrane component.  (+info)

Transforming growth factor-beta induces formation of a dithiothreitol-resistant type I/Type II receptor complex in live cells. (5/2188)

Transforming growth factor-beta (TGF-beta) binds to and signals via two serine-threonine kinase receptors, the type I (TbetaRI) and type II (TbetaRII) receptors. We have used different and complementary techniques to study the physical nature and ligand dependence of the complex formed by TbetaRI and TbetaRII. Velocity centrifugation of endogenous receptors suggests that ligand-bound TbetaRI and TbetaRII form a heteromeric complex that is most likely a heterotetramer. Antibody-mediated immunofluorescence co-patching of epitope-tagged receptors provides the first evidence in live cells that TbetaRI. TbetaRII complex formation occurs at a low but measurable degree in the absence of ligand, increasing significantly after TGF-beta binding. In addition, we demonstrate that pretreatment of cells with dithiothreitol, which inhibits the binding of TGF-beta to TbetaRI, does not prevent formation of the TbetaRI.TbetaRII complex, but increases its sensitivity to detergent and prevents TGF-beta-activated TbetaRI from phosphorylating Smad3 in vitro. This indicates that either a specific conformation of the TbetaRI. TbetaRII complex, disrupted by dithiothreitol, or direct binding of TGF-beta to TbetaRI is required for signaling.  (+info)

Gamma-Actinin, a new regulatory protein from rabbit skeletal muscle. I. Purification and characterization. (6/2188)

A new regulatory protein which we have designated as gamma-actinin has been isolated from native thin filaments of rabbit skeletal muscle. Depolymerized native thin filaments were fractionated by salting out with ammonium sulfate, and the precipitates obtained at 40--60% ammonium sulfate saturation were further subjected to DEAE-Sephadex and Sephadex G-200 column chromatography. The purified gamma-actinin was shown to have a chain weight of 35,000 daltons and had a strong inhibitory action on the polymerization of G-actin. The results of amino acid analysis indicated a unique amino acid composition of gamma-actinin as compared with other structural proteins of muscle. Non-polar and neutral amino acid residues were abundant. One cysteine residue was contained per one molecule of gamma-actinin and played a critical role in the maintenance of the inhibitory activity. Pelleting of gamma-actinin with F-actin showed that gamma-actinin binds to F-action.  (+info)

Phospholipid hydroperoxide cysteine peroxidase activity of human serum albumin. (7/2188)

Human serum albumin (HSA) reduced the phospholipid hydroperoxide, 1-palmitoyl-2-(13-hydroperoxy-cis-9, trans-11-octadecadienoyl)-l-3-phosphatidylcholine (PLPC-OOH) to the corresponding hydroxy-derivative with a high apparent affinity (Km=9. 23+/-0.95 microM). Removal of bound lipid during purification increased this activity. At physiological concentration, HSA reduced the phospholipid hydroperoxide in the absence of a cofactor. However, in the presence of a cofactor (reductant), the rate of the reaction was increased. All of the major aminothiols in plasma could act as reductants, the best being the most abundant, cysteine (Km=600+/-80 microM). For every nanomole of PLPC-OOH reduced by HSA, 1.26 nmol of cystine was formed, indicating a reaction stoichiometry of 1 mol PLPC-OOH to 2 mol cysteine. We used chemical modification to determine which amino acid residues on HSA were responsible for the activity. Oxidation of thiol group(s) by N-ethylmaleimide led to a reduction in the rate of activity, whereas reduction of thiols by either dithiothreitol or the angiotensin-converting enzyme inhibitor, captopril, increased the activity. Both N-ethylmaleimide-modified HSA and dithiothreitol-treated HSA exhibited increased apparent affinities for PLPC-OOH. For a range of preparations of albumin with different modifications, the activity on PLPC-OOH was dependent on the amount of free thiol groups on the albumin (correlation coefficient=0.91). Patients with lowered albumin concentrations after septic shock showed lowered total plasma thiol concentrations and decreased phospholipid hydroperoxide cysteine peroxidase (PHCPx) activities. These results therefore show for the first time that HSA exhibits PHCPx activity, and that the majority of the activity depends on the presence of reduced thiol group(s) on the albumin.  (+info)

Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway. (8/2188)

Escherichia coli DsbB has four essential cysteine residues, among which Cys41 and Cys44 form a CXXC redox active site motif and the Cys104-Cys130 disulfide bond oxidizes the active site cysteines of DsbA, the disulfide bond formation factor in the periplasm. Functional respiratory chain is required for the cell to keep DsbA oxidized. In this study, we characterized the roles of essential cysteines of DsbB in the coupling with the respiratory chain. Cys104 was found to form the inactive complex with DsbA under respiration-defective conditions. While DsbB, under normal aerobic conditions, is in the oxidized state, having two intramolecular disulfide bonds, oxidation of Cys104 and Cys130 requires the presence of Cys41-Cys44. Remarkably, the Cys41-Cys44 disulfide bond is refractory to reduction by a high concentration of dithiothreitol, unless the membrane is solubilized with a detergent. This reductant resistance requires both the respiratory function and oxygen, since Cys41-Cys44 became sensitive to the reducing agent when membrane was prepared from quinone- or heme-depleted cells or when a membrane sample was deaerated. Thus, the Cys41-Val-Leu-Cys44 motif of DsbB is kept both strongly oxidized and strongly oxidizing when DsbB is integrated into the membrane with the normal set of respiratory components.  (+info)

Dithiothreitol (DTT) is a reducing agent used in various medical and scientific applications. It is a small molecule that contains two sulfur atoms and is commonly used to break disulfide bonds in proteins, which can help to unfold or denature them. This property makes DTT useful in protein purification and analysis, as well as in the study of protein structure and function. In addition to its use in protein chemistry, DTT is also used in the treatment of certain medical conditions. For example, it has been shown to have anti-inflammatory and antioxidant effects, and it has been used to treat conditions such as cystic fibrosis and multiple sclerosis. However, more research is needed to fully understand the potential therapeutic applications of DTT in medicine.

Sulfhydryl compounds are organic compounds that contain a sulfur atom bonded to a hydrogen atom. They are also known as thiol compounds. In the medical field, sulfhydryl compounds are important because they play a role in many biological processes, including metabolism, detoxification, and antioxidant defense. They are also used in the treatment of certain medical conditions, such as heart disease and diabetes. Some examples of sulfhydryl compounds include cysteine, glutathione, and methionine.

In the medical field, disulfides refer to chemical compounds that contain two sulfur atoms connected by a single bond. Disulfides are commonly found in proteins, where they play an important role in maintaining the structure and function of the protein. One of the most well-known examples of a disulfide is the cystine molecule, which is composed of two cysteine amino acids that are linked together by a disulfide bond. Disulfide bonds are important for the proper folding and stability of proteins, and they can also play a role in the function of the protein. Disulfides can also be found in other types of molecules, such as lipids and carbohydrates. In these cases, disulfides may play a role in the structure and function of the molecule, or they may be involved in signaling pathways within the body. Overall, disulfides are an important class of chemical compounds that play a variety of roles in the body, including the maintenance of protein structure and function, and the regulation of signaling pathways.

Mercaptoethanol is a chemical compound that is used in the medical field as a reducing agent. It is a derivative of ethanol (alcohol) that contains a sulfur atom (-SH) attached to one of its carbon atoms. Mercaptoethanol is often used in the treatment of certain genetic disorders, such as sickle cell anemia and thalassemia, by reducing the levels of abnormal hemoglobin in the blood. It is also used in the production of certain vaccines and as a preservative in some medical products. Mercaptoethanol is a toxic substance and should be handled with care by medical professionals.

Cysteine is an amino acid that is essential for the proper functioning of the human body. It is a sulfur-containing amino acid that is involved in the formation of disulfide bonds, which are important for the structure and function of many proteins. Cysteine is also involved in the detoxification of harmful substances in the body, and it plays a role in the production of glutathione, a powerful antioxidant. In the medical field, cysteine is used to treat a variety of conditions, including respiratory infections, kidney stones, and cataracts. It is also used as a dietary supplement to support overall health and wellness.

Ethylmaleimide is a chemical compound that is used in the medical field as a research tool to study the function of enzymes involved in the synthesis and breakdown of proteins. It works by inhibiting an enzyme called peptidyl-prolyl cis-trans isomerase (PPIase), which is involved in the folding and stability of proteins. By inhibiting PPIase, ethylmaleimide can be used to study the role of this enzyme in various cellular processes and diseases, such as cancer, neurodegenerative disorders, and autoimmune diseases. Ethylmaleimide is also used as a chemical probe to study the structure and function of proteins, particularly those involved in signal transduction pathways.

Dithionitrobenzoic acid (DTNB) is a chemical compound that is commonly used in medical research and diagnostic tests. It is a yellowish-orange solid that is highly soluble in water and polar organic solvents. In the medical field, DTNB is often used as a reagent in the detection of thiols, which are a class of organic compounds that contain a sulfur atom with a negative charge. Thiols are found in many biological molecules, including enzymes, hormones, and antioxidants, and their presence can be important for the proper functioning of these molecules. DTNB reacts with thiols to form a yellow-colored product called 5,5'-dithiobis(2-nitrobenzoic acid), which can be easily detected and quantified. This reaction is often used in diagnostic tests to measure the concentration of thiols in biological samples, such as blood, urine, and tissue extracts. In addition to its use in diagnostic tests, DTNB has also been used in research to study the structure and function of proteins, as well as the mechanisms of various biological processes.

In the medical field, diamide refers to a class of compounds that contain two amide groups (-CONH-) attached to a central atom. Diamides are often used as drugs or as intermediates in the synthesis of other drugs. One example of a diamide drug is metformin, which is used to treat type 2 diabetes. Metformin works by inhibiting the enzyme responsible for the production of glucose in the liver, which helps to lower blood sugar levels. Diamides can also be used as herbicides, insecticides, and fungicides. For example, the diamide herbicide imazamox is used to control grassy weeds in cereal crops, while the diamide insecticide chlorantraniliprole is used to control a variety of pests in crops such as cotton, corn, and soybeans. Overall, diamides are a versatile class of compounds with a range of applications in medicine and agriculture.

Glutathione is a naturally occurring antioxidant that is produced by the body. It is a tripeptide composed of three amino acids: cysteine, glycine, and glutamic acid. Glutathione plays a crucial role in protecting cells from damage caused by free radicals, which are unstable molecules that can damage cells and contribute to the development of diseases such as cancer, heart disease, and neurodegenerative disorders. In the medical field, glutathione is often used as a supplement to support the immune system and protect against oxidative stress. It is also used in the treatment of certain conditions, such as liver disease, HIV/AIDS, and cancer. However, more research is needed to fully understand the potential benefits and risks of glutathione supplementation.

Iodobenzoates are a class of organic compounds that contain an iodine atom bonded to a benzoic acid group. They are commonly used as antiseptics and disinfectants in the medical field. One example of an iodobenzoate is povidone-iodine, which is a solution of polyvinylpyrrolidone (PVP) and iodine. Povidone-iodine is commonly used as a topical antiseptic for skin wounds, burns, and other infections. It is also used as a disinfectant for surfaces and medical equipment. Other iodobenzoates, such as chlorhexidine gluconate and benzalkonium chloride, are also used in the medical field as antiseptics and disinfectants. Chlorhexidine gluconate is commonly used as a mouthwash and throat lozenge to treat infections of the mouth and throat. Benzalkonium chloride is used as a disinfectant for surfaces and medical equipment.

Iodoacetamide is a chemical compound that is commonly used in the medical field as a contrast agent for diagnostic imaging. It is a white, crystalline solid that is soluble in water and other polar solvents. When injected into the body, it is taken up by cells and tissues, and its presence can be detected using imaging techniques such as computed tomography (CT) scans or magnetic resonance imaging (MRI). Iodoacetamide is also used as a reagent in laboratory experiments to label proteins and other molecules with radioactive iodine.

Thioredoxins are a family of small, redox-active proteins that are found in all living organisms. They are involved in a wide range of cellular processes, including the regulation of gene expression, the detoxification of reactive oxygen species, and the maintenance of cellular redox homeostasis. Thioredoxins contain a conserved active site that contains a disulfide bond, which can be reduced or oxidized depending on the cellular redox state. This allows thioredoxins to participate in redox reactions, in which they transfer electrons from one molecule to another. In the medical field, thioredoxins have been studied for their potential therapeutic applications. For example, they have been shown to have anti-inflammatory and anti-cancer effects, and they may be useful in the treatment of a variety of diseases, including cardiovascular disease, neurodegenerative disorders, and cancer.

Chloromercuribenzoates are a class of organic compounds that contain a mercury atom bonded to a chloro group and a benzoate group. They are used as antiseptics and disinfectants in the medical field. Chloromercuribenzoates are effective against a wide range of microorganisms, including bacteria, viruses, and fungi. They are commonly used in the treatment of skin infections, eye infections, and other types of infections. However, they can also be toxic to humans and animals, and their use is therefore restricted in some countries.

Hydroxymercuribenzoates are a class of organic compounds that contain a mercury atom bonded to a hydroxyl group and a benzoate group. They are used as antiseptics and disinfectants in the medical field. One example of a hydroxymercuribenzoate is mercurochrome, which was commonly used as a topical antiseptic in the past but has been banned in many countries due to concerns about its toxicity. Other hydroxymercuribenzoates, such as chlorhexidine, are still widely used in healthcare settings for their antimicrobial properties.

Thimerosal is a mercury-based preservative that has been used in vaccines and other medical products to prevent the growth of bacteria and fungi. It is typically added to vaccines in very small amounts, typically less than 1 part per million (ppm), to prevent contamination and extend the shelf life of the vaccine. Thimerosal has been the subject of controversy in recent years, with some people raising concerns about its safety and potential health effects. However, the vast majority of scientific research has found that thimerosal is safe and effective when used in recommended doses. The U.S. Centers for Disease Control and Prevention (CDC) and the World Health Organization (WHO) both recommend the use of vaccines containing thimerosal to help prevent the spread of infectious diseases. It is important to note that the amount of thimerosal in vaccines is much lower than the amount that would be considered harmful if ingested or absorbed by the body. The CDC and other health organizations have stated that the small amounts of thimerosal used in vaccines pose no significant risk to human health.

Dithioerythritol (DTE) is a chemical compound that is used in the medical field as a contrast agent for magnetic resonance imaging (MRI). It is a paramagnetic molecule that has two sulfur atoms in its structure, which interact with the magnetic field of the MRI machine and enhance the contrast between different tissues in the body. DTE is typically administered intravenously and is used to enhance the contrast of certain organs and tissues, such as the liver, spleen, and kidneys. It is also used to diagnose and monitor certain medical conditions, such as liver disease, kidney disease, and cancer. DTE is generally considered safe and well-tolerated, although it can cause some side effects, such as nausea, vomiting, and headache. It is important to note that DTE is not suitable for everyone, and patients should always discuss the potential risks and benefits with their healthcare provider before undergoing an MRI with DTE contrast.

Edetic acid, also known as ethylenediaminetetraacetic acid (EDTA), is a synthetic organic acid that is commonly used in the medical field as a chelating agent. It is a colorless, water-soluble solid that is used to dissolve minerals and other metal ions in solution. In medicine, EDTA is often used to treat heavy metal poisoning, such as lead or mercury poisoning, by binding to the metal ions and facilitating their excretion from the body. It is also used as an anticoagulant in blood tests and as a component of certain contrast agents used in diagnostic imaging procedures. EDTA is available in various forms, including tablets, capsules, and intravenous solutions. It is generally considered safe when used as directed, but high doses or prolonged use can cause side effects such as nausea, vomiting, and allergic reactions.

Glutathione disulfide (GSSG) is a molecule that is formed when two molecules of glutathione (GSH) are linked together by a disulfide bond. Glutathione is a powerful antioxidant that is found in all cells of the body and plays a crucial role in protecting cells from damage caused by free radicals. GSSG is the oxidized form of glutathione and is converted back to its reduced form, GSH, by an enzyme called glutathione reductase. In the medical field, GSSG is often used as a biomarker of oxidative stress, as levels of GSSG in the body are thought to be higher in individuals with certain diseases or conditions that are associated with increased oxidative stress.

Hydrogen peroxide (H2O2) is a colorless, odorless liquid that is commonly used in the medical field as a disinfectant, antiseptic, and oxidizing agent. It is a strong oxidizing agent that can break down organic matter, including bacteria, viruses, and fungi, making it useful for disinfecting wounds, surfaces, and medical equipment. In addition to its disinfectant properties, hydrogen peroxide is also used in wound care to remove dead tissue and promote healing. It is often used in combination with other wound care products, such as saline solution or antibiotic ointment, to help prevent infection and promote healing. Hydrogen peroxide is also used in some medical procedures, such as endoscopy and bronchoscopy, to help clean and disinfect the equipment before use. It is also used in some dental procedures to help remove stains and whiten teeth. However, it is important to note that hydrogen peroxide can be harmful if not used properly. It should not be ingested or applied directly to the skin or mucous membranes without first diluting it with water. It should also be stored in a cool, dry place away from children and pets.

In the medical field, macromolecular substances refer to large molecules that are composed of repeating units, such as proteins, carbohydrates, lipids, and nucleic acids. These molecules are essential for many biological processes, including cell signaling, metabolism, and structural support. Macromolecular substances are typically composed of thousands or even millions of atoms, and they can range in size from a few nanometers to several micrometers. They are often found in the form of fibers, sheets, or other complex structures, and they can be found in a variety of biological tissues and fluids. Examples of macromolecular substances in the medical field include: - Proteins: These are large molecules composed of amino acids that are involved in a wide range of biological functions, including enzyme catalysis, structural support, and immune response. - Carbohydrates: These are molecules composed of carbon, hydrogen, and oxygen atoms that are involved in energy storage, cell signaling, and structural support. - Lipids: These are molecules composed of fatty acids and glycerol that are involved in energy storage, cell membrane structure, and signaling. - Nucleic acids: These are molecules composed of nucleotides that are involved in genetic information storage and transfer. Macromolecular substances are important for many medical applications, including drug delivery, tissue engineering, and gene therapy. Understanding the structure and function of these molecules is essential for developing new treatments and therapies for a wide range of diseases and conditions.

Dimercaprol, also known as British Anti-Lewisite (BAL), is a medication used to treat heavy metal poisoning, particularly from arsenic, mercury, and thallium. It works by binding to the heavy metal ions and facilitating their excretion from the body through the kidneys. Dimercaprol is typically administered intravenously and can cause side effects such as nausea, vomiting, and allergic reactions. It is not recommended for use in patients with certain medical conditions, such as kidney or liver disease, or during pregnancy.

p-Chloromercuribenzoic acid (p-CMB) is a medication that was once used to treat certain types of skin conditions, such as psoriasis and eczema. It works by slowing down the growth of skin cells and reducing inflammation. However, p-CMB has been found to be toxic to the liver and kidneys, and its use has been largely discontinued. It is not currently recommended for use in the medical field.

S-Nitrosoglutathione (GSNO) is a naturally occurring molecule in the body that plays a role in the regulation of various physiological processes, including vasodilation, neurotransmission, and antioxidant defense. It is formed by the reaction of nitric oxide (NO) with glutathione (GSH), a tripeptide composed of glutamate, cysteine, and glycine. GSNO is a potent vasodilator, meaning it can cause blood vessels to widen, which can help to lower blood pressure and improve blood flow. It also plays a role in neurotransmission, as it can modulate the activity of certain neurotransmitters in the brain. Additionally, GSNO acts as an antioxidant, helping to protect cells from damage caused by reactive oxygen species. In the medical field, GSNO has been studied for its potential therapeutic applications in a variety of conditions, including cardiovascular disease, neurodegenerative disorders, and cancer. However, more research is needed to fully understand the role of GSNO in these conditions and to determine its safety and efficacy as a treatment.

Cystamine is a naturally occurring diamine compound that is found in various plants and animals. In the medical field, cystamine is used as a medication to treat certain types of cystic fibrosis and other lung diseases. It works by reducing the production of mucus in the lungs, which can help to improve breathing and reduce the risk of infections. Cystamine is also being studied for its potential use in treating other conditions, such as cancer and neurodegenerative diseases. It is usually administered as a capsule or solution by mouth, and the dosage and duration of treatment will depend on the specific condition being treated.

Iodoacetates are a class of organic compounds that contain a carbonyl group (-CO-) and an iodine atom (-I). They are commonly used in the medical field as contrast agents for diagnostic imaging, particularly in the field of radiology. One specific example of an iodoacetate is iodoacetamide, which is used as a radiopaque agent for imaging of the kidneys and urinary tract. It works by binding to the cysteine residues on the surface of cells in the kidneys and urinary tract, making them visible on X-ray images. Iodoacetates can also be used as antiseptics and disinfectants, and as intermediates in the synthesis of other organic compounds. However, they can be toxic if ingested or inhaled in large quantities, and can cause irritation and damage to the skin, eyes, and respiratory system.

Phosphorous acids are a group of compounds that contain a phosphorus atom bonded to one or more hydroxyl (-OH) groups. They are commonly used in the medical field as intermediates in the synthesis of various pharmaceuticals and as components in certain diagnostic tests. One example of a phosphorous acid used in medicine is phosphoric acid, which is a weak acid that is commonly used as an ingredient in various medications, including antacids and laxatives. It is also used as a preservative in some medical solutions and as a buffer in certain diagnostic tests. Other phosphorous acids that are used in medicine include orthophosphoric acid, which is used as a component in certain diagnostic tests and as a preservative in some medical solutions, and pyrophosphoric acid, which is used as a component in certain medications and as a buffer in certain diagnostic tests. Phosphorous acids can also be used in the treatment of certain medical conditions, such as osteoporosis, where they can help to increase bone density and reduce the risk of fractures. They may also be used in the treatment of certain skin conditions, such as psoriasis, where they can help to reduce inflammation and improve skin health.

Amino acids are organic compounds that are the building blocks of proteins. They are composed of an amino group (-NH2), a carboxyl group (-COOH), and a side chain (R group) that varies in size and structure. There are 20 different amino acids that are commonly found in proteins, each with a unique side chain that gives it distinct chemical and physical properties. In the medical field, amino acids are important for a variety of functions, including the synthesis of proteins, enzymes, and hormones. They are also involved in energy metabolism and the maintenance of healthy tissues. Deficiencies in certain amino acids can lead to a range of health problems, including muscle wasting, anemia, and neurological disorders. In some cases, amino acids may be prescribed as supplements to help treat these conditions or to support overall health and wellness.

Adenosine triphosphate (ATP) is a molecule that serves as the primary energy currency in living cells. It is composed of three phosphate groups attached to a ribose sugar and an adenine base. In the medical field, ATP is essential for many cellular processes, including muscle contraction, nerve impulse transmission, and the synthesis of macromolecules such as proteins and nucleic acids. ATP is produced through cellular respiration, which involves the breakdown of glucose and other molecules to release energy that is stored in the bonds of ATP. Disruptions in ATP production or utilization can lead to a variety of medical conditions, including muscle weakness, fatigue, and neurological disorders. In addition, ATP is often used as a diagnostic tool in medical testing, as levels of ATP can be measured in various bodily fluids and tissues to assess cellular health and function.

Trypsin is a proteolytic enzyme that is produced by the pancreas and is responsible for breaking down proteins into smaller peptides and amino acids. It is a serine protease that cleaves peptide bonds on the carboxyl side of lysine and arginine residues. Trypsin is an important digestive enzyme that helps to break down dietary proteins into smaller peptides and amino acids that can be absorbed and used by the body. It is also used in medical research and in the development of diagnostic tests and therapeutic agents.

Cystine is a sulfur-containing amino acid that is an essential component of proteins. It is a dipeptide composed of two cysteine amino acids linked together by a disulfide bond. In the medical field, cystine is known to play a role in the formation of cystine stones in the urinary tract. These stones can cause significant pain and discomfort, and may require medical intervention to remove. Cystine is also involved in the structure and function of certain proteins, including enzymes and structural proteins. It is an important nutrient for the body, and is found in a variety of foods, including meat, poultry, fish, and dairy products.

NADP stands for Nicotinamide Adenine Dinucleotide Phosphate. It is a coenzyme that plays a crucial role in various metabolic processes in the body, including the metabolism of carbohydrates, fats, and proteins. NADP is involved in the conversion of glucose to glycogen, the breakdown of fatty acids, and the synthesis of amino acids. It is also involved in the process of photosynthesis in plants, where it acts as a carrier of electrons. In the medical field, NADP is often used as a supplement to support various metabolic processes and to enhance energy production in the body.

In the medical field, "Cations, Divalent" refers to positively charged ions that have a charge of +2. These ions are typically metal ions, such as calcium, magnesium, and zinc, and are important for various physiological processes in the body. Divalent cations play a crucial role in maintaining the balance of electrolytes in the body, which is essential for proper nerve and muscle function. They are also involved in bone health, as calcium and magnesium are important components of bone tissue. Imbalances in the levels of divalent cations can lead to a variety of health problems, including muscle cramps, seizures, and heart arrhythmias. In some cases, medications may be prescribed to help regulate the levels of these ions in the body.

In the medical field, nitroso compounds are a class of chemical compounds that contain a nitroso group (-NO) attached to a carbon atom. These compounds are commonly found in the environment and in certain foods, such as bacon and processed meats. There are two main types of nitroso compounds: primary nitroso compounds and secondary nitroso compounds. Primary nitroso compounds are formed when a nitrite ion (NO2-) reacts with an amine (NH2-) to form a nitrosamine. Secondary nitroso compounds are formed when a nitrite ion reacts with an aldehyde or ketone to form a nitrosylamine. Nitroso compounds can be toxic to humans and have been linked to various health problems, including cancer. Some nitroso compounds can also react with certain enzymes in the body to form reactive nitrogen species, which can damage cells and DNA. As a result, the consumption of nitroso compounds in certain foods has been linked to an increased risk of certain types of cancer, such as stomach cancer.

Magnesium is a mineral that is essential for many bodily functions. It is involved in over 300 enzymatic reactions in the body, including the production of energy, the synthesis of proteins and DNA, and the regulation of muscle and nerve function. In the medical field, magnesium is used to treat a variety of conditions, including: 1. Hypomagnesemia: A deficiency of magnesium in the blood. This can cause symptoms such as muscle cramps, spasms, and seizures. 2. Cardiac arrhythmias: Abnormal heart rhythms that can be caused by low levels of magnesium. 3. Pre-eclampsia: A condition that can occur during pregnancy and is characterized by high blood pressure and protein in the urine. Magnesium supplementation may be used to treat this condition. 4. Chronic kidney disease: Magnesium is often lost in the urine of people with chronic kidney disease, and supplementation may be necessary to maintain adequate levels. 5. Alcohol withdrawal: Magnesium supplementation may be used to treat symptoms of alcohol withdrawal, such as tremors and seizures. 6. Muscle spasms: Magnesium can help to relax muscles and relieve spasms. 7. Anxiety and depression: Some studies have suggested that magnesium supplementation may help to reduce symptoms of anxiety and depression. Magnesium is available in various forms, including oral tablets, capsules, and intravenous solutions. It is important to note that high levels of magnesium can also be toxic, so it is important to use magnesium supplements under the guidance of a healthcare provider.

Calcium is a chemical element with the symbol Ca and atomic number 20. It is a vital mineral for the human body and is essential for many bodily functions, including bone health, muscle function, nerve transmission, and blood clotting. In the medical field, calcium is often used to diagnose and treat conditions related to calcium deficiency or excess. For example, low levels of calcium in the blood (hypocalcemia) can cause muscle cramps, numbness, and tingling, while high levels (hypercalcemia) can lead to kidney stones, bone loss, and other complications. Calcium supplements are often prescribed to people who are at risk of developing calcium deficiency, such as older adults, vegetarians, and people with certain medical conditions. However, it is important to note that excessive calcium intake can also be harmful, and it is important to follow recommended dosages and consult with a healthcare provider before taking any supplements.

Chloroplast thioredoxins are a group of small, soluble proteins that are found in the chloroplasts of plants and algae. They are involved in a variety of cellular processes, including photosynthesis, the regulation of gene expression, and the detoxification of reactive oxygen species. Thioredoxins are a type of antioxidant that contain a disulfide bond, which can be reduced or oxidized depending on the cellular redox state. In the reduced state, thioredoxins are able to donate electrons to other molecules, while in the oxidized state, they can accept electrons from other molecules. Chloroplast thioredoxins are thought to play a role in the regulation of photosynthesis by controlling the activity of enzymes involved in the process. They may also be involved in the response of plants to environmental stress, such as exposure to high levels of light or drought. Overall, chloroplast thioredoxins are important for the proper functioning of chloroplasts and the overall health of plants and algae.

Isomerases are a class of enzymes that catalyze the interconversion of isomers, which are molecules with the same molecular formula but different arrangements of atoms. In the medical field, isomerases are important because they play a role in many biological processes, including metabolism, signal transduction, and gene expression. There are several types of isomerases, including: 1. Stereoisomerases: These enzymes catalyze the interconversion of stereoisomers, which are molecules with the same molecular formula and connectivity but different spatial arrangements of atoms. Examples of stereoisomerases include epimerases, which interconvert epimers (stereoisomers that differ in configuration at a single chiral center), and diastereomerases, which interconvert diastereomers (stereoisomers that differ in configuration at two or more chiral centers). 2. Conformational isomerases: These enzymes catalyze the interconversion of conformational isomers, which are molecules with the same molecular formula and connectivity but different three-dimensional structures. Examples of conformational isomerases include chaperones, which assist in the folding and unfolding of proteins, and peptidyl-prolyl cis-trans isomerases, which catalyze the interconversion of cis and trans isomers of proline residues in peptides and proteins. 3. Metabolic isomerases: These enzymes catalyze the interconversion of metabolic isomers, which are molecules that are involved in metabolic pathways. Examples of metabolic isomerases include aldolases, which catalyze the reversible cleavage of aldoses into ketoses and aldehydes, and transketolases, which catalyze the transfer of a keto group from one aldose to another. Isomerases are important in the medical field because they can be targeted for the treatment of diseases. For example, some drugs target specific isomerases to treat metabolic disorders, such as diabetes and obesity, and some drugs target isomerases to treat cancer, such as by inhibiting the activity of enzymes involved in the metabolism of cancer cells.

In the medical field, peroxides are chemical compounds that contain the oxygen-oxygen (O-O) bond. They are commonly used as disinfectants, bleaching agents, and oxidizing agents in various medical applications. One of the most well-known peroxides in medicine is hydrogen peroxide (H2O2), which is used as a topical antiseptic to clean wounds and prevent infection. Hydrogen peroxide is also used as a mouthwash to treat gum disease and other oral infections. Other peroxides used in medicine include peroxyacetic acid (PAA), which is used as a disinfectant for medical equipment and surfaces, and peroxynitrite (ONOO-), which is a potent oxidizing agent that plays a role in the body's immune response. Peroxides can also be used in the treatment of certain medical conditions, such as the use of ozone therapy to treat chronic pain and other inflammatory conditions. However, the use of peroxides in medicine should be carefully monitored and controlled to avoid potential side effects and complications.

Protein Disulfide-Isomerases (PDIs) are a family of enzymes that play a crucial role in the folding and assembly of proteins in the endoplasmic reticulum (ER) of eukaryotic cells. PDIs catalyze the formation, breakage, and rearrangement of disulfide bonds within proteins, which are essential for maintaining their three-dimensional structure and function. In the medical field, PDIs are of great interest due to their involvement in various diseases, including neurodegenerative disorders, cancer, and infectious diseases. For example, PDIs have been implicated in the formation of toxic protein aggregates that are associated with diseases such as Alzheimer's, Parkinson's, and Huntington's disease. PDIs have also been shown to play a role in the folding and assembly of viral proteins, making them potential targets for antiviral therapies. In addition, PDIs have been used as therapeutic agents in their own right. For example, PDI inhibitors have been shown to have anti-cancer activity by disrupting the folding and assembly of proteins involved in cancer cell proliferation and survival. PDIs have also been used as a tool to study protein folding and assembly, as well as to develop new methods for protein engineering and drug discovery.

Oxidoreductases are a class of enzymes that catalyze redox reactions, which involve the transfer of electrons from one molecule to another. These enzymes play a crucial role in many biological processes, including metabolism, energy production, and detoxification. In the medical field, oxidoreductases are often studied in relation to various diseases and conditions. For example, some oxidoreductases are involved in the metabolism of drugs and toxins, and changes in their activity can affect the efficacy and toxicity of these substances. Other oxidoreductases are involved in the production of reactive oxygen species (ROS), which can cause cellular damage and contribute to the development of diseases such as cancer and aging. Oxidoreductases are also important in the diagnosis and treatment of certain diseases. For example, some oxidoreductases are used as markers of liver disease, and changes in their activity can indicate the severity of the disease. In addition, some oxidoreductases are targets for drugs used to treat diseases such as cancer and diabetes. Overall, oxidoreductases are a diverse and important class of enzymes that play a central role in many biological processes and are the subject of ongoing research in the medical field.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

Mersalyl is a medication that is used to treat infections caused by certain types of bacteria. It is a type of antibiotic that belongs to the class of drugs known as quinolones. Mersalyl is typically used to treat infections of the urinary tract, respiratory tract, and skin. It is usually taken by mouth, although it can also be given intravenously in some cases. Mersalyl is not effective against infections caused by viruses, such as the flu or common cold. It is important to follow the instructions of your healthcare provider when taking Mersalyl, as it can cause side effects such as nausea, diarrhea, and headache.

NAD stands for nicotinamide adenine dinucleotide, which is a coenzyme found in all living cells. It plays a crucial role in various metabolic processes, including energy production, DNA repair, and regulation of gene expression. In the medical field, NAD is often used as a supplement to support cellular health and improve overall well-being. It is also being studied for its potential therapeutic applications in treating conditions such as depression, anxiety, and chronic pain.

Peroxidases are a group of enzymes that catalyze the oxidation of various substrates using hydrogen peroxide as the oxidizing agent. In the medical field, peroxidases are commonly used as diagnostic tools to detect the presence of specific substances in biological samples, such as blood, urine, or tissue. One of the most well-known peroxidases in medicine is the enzyme lactoperoxidase, which is found in high concentrations in human milk. Lactoperoxidase plays a crucial role in protecting the newborn from bacterial and viral infections by generating antimicrobial compounds. Another important peroxidase in medicine is the enzyme myeloperoxidase, which is produced by white blood cells (neutrophils) and is involved in the immune response against infections. Myeloperoxidase is often used as a marker of inflammation in various medical conditions, such as chronic obstructive pulmonary disease (COPD), rheumatoid arthritis, and inflammatory bowel disease. Peroxidases are also used in forensic science to analyze biological samples for evidence in criminal investigations. For example, the enzyme cytochrome c peroxidase can be used to detect the presence of blood at a crime scene, while the enzyme glucose oxidase is used to detect the presence of glucose in urine samples.

4-Chloromercuribenzenesulfonate (4-CMBS) is a chemical compound that contains a mercury atom bonded to a chlorine atom and a benzenesulfonate group. It is used in the medical field as a diagnostic tool for detecting the presence of mercury in the body. 4-CMBS is typically administered to a patient orally or intravenously, and the mercury in the body is then converted to a radioactive form that can be detected using a gamma camera. This test is commonly used to diagnose mercury poisoning, which can occur as a result of exposure to mercury in various forms, such as mercury vapor, mercury-contaminated water, or mercury-containing products. It is important to note that 4-CMBS is a radioactive compound and should only be administered by a qualified healthcare professional in a controlled setting. Additionally, the use of 4-CMBS may not be appropriate for all patients, and other diagnostic tests may be more appropriate in certain cases.

... (DTT) is the common name for a small-molecule redox reagent also known as Cleland's reagent, after W. Wallace ... Dithiothreitol shelf life can be extended with refrigeration at 2-8 °C. Oxidation presents further complications as oxidized ... ISBN 0-911910-13-1. Cleland WW (April 1964). "Dithiothreitol, a New Protective Reagent for SH Groups". Biochemistry. 3 (4): 480 ... doi:10.1016/0307-4412(83)90048-1. Media related to Dithiothreitol at Wikimedia Commons (Articles without KEGG source, Articles ...
1976). "Reaction of rhodanese with dithiothreitol". Biochim. Biophys. Acta. 445 (1): 104-11. doi:10.1016/0005-2744(76)90163-7. ...
It is an epimer of dithiothreitol (DTT). The molecular formula for DTE is C4H10O2S2. DTE is a crystalline solid soluble in ... Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH Groups". Biochemistry. 3 (4): 480-2. doi:10.1021/ ...
Recipe: 0.5% (w/v) SDS 0.05 M Tris⋅Cl Adjust pH to 8.0 Add 1 mM fresh dithiothreitol (DTT) ACK is used for lysis of red blood ... and reducing agents like dithiothreitol (DTT). It may be the most widely used lysis buffer. The solubilizing agent is NP-40, ...
It also binds the sulfate ion and dithiothreitol. Maleylacetoacetate isomerase deficiency is a disease caused by a mutation in ...
biographical article Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH Groups". Biochemistry. 3 (4 ...
This enzyme has at least one effector, Dithiothreitol. Liau YH, Slomiany BL, Slomiany A, Piasek A, Palmer D, Rosenthal WS (1985 ...
He was the first to use dithiothreitol for the reduction of disulfide bonds in proteins, and the compound is accordingly often ... Cleland, W.W. (April 1964). "Dithiothreitol, A New Protective Reagent for SH Groups". Biochemistry. 3 (4): 480-2. doi:10.1021/ ...
Dithiothreitol (DTT) 2-Mercaptoethanol (BME) TCEP Lukesh, John C.; Palte, Michael J.; Raines, Ronald T. (2012-02-21). "A Potent ...
It has 3 cofactors: pyridoxal phosphate, Cobamide coenzyme, and Dithiothreitol. Somack R, Costilow RN (1973). "Purification and ...
The thiols are then reduced with dithiothreitol and labelled by monobromobimane. Monobromobimane becomes fluorescent after ...
If this is not effective, dithiothreitol can be used to destroy the antibodies.: 141 Cord blood samples may be contaminated ...
Reducing conditions are usually maintained by the addition of beta-mercaptoethanol or dithiothreitol. For a general analysis of ...
Dithiothreitol will slowly over time absorb more and more light in this spectrum as various redox reactions occur. Reduction of ... TCEP can keep the cysteines from forming di-sulfide bonds and, unlike dithiothreitol and β-mercaptoethanol, it will not react ... 2-Mercaptoethanol (BME) Dithiothreitol (DTT) Dithiobutylamine (DTBA) Ruegg, U.T & Rudinger, J. (1977). "Reductive cleavage of ... Compared to the other two most common agents used for this purpose (dithiothreitol and β-mercaptoethanol), TCEP has the ...
OPAA activity is enhanced by reducing agents such as dithiothreitol (DTT) and beta-mercaptoethanol. OPAA is also catalytically ...
In biochemistry, thiols such as β-mercaptoethanol (β-ME) or dithiothreitol (DTT) serve as reductants; the thiol reagents are ... Typically, the thiolate of a redox reagent such as glutathione or dithiothreitol attacks the disulfide bond on a protein ...
A23187 upregulates expression of ER stress proteins 2-deoxyglucose dithiothreitol reduces the disulfide bridges of proteins. ...
The sources of reducing power for GPx-3 in vitro include GSH, cysteine, mercaptoethanol, and dithiothreitol. There is an ...
Dithiothreitol (DTT) Dithiobutylamine (DTBA) TCEP Nomenclature of Organic Chemistry : IUPAC Recommendations and Preferred Names ... However, since 2-mercaptoethanol forms adducts with free cysteines and is somewhat more toxic, dithiothreitol (DTT) is ... 2-Mercaptoethanol is often used interchangeably with dithiothreitol (DTT) or the odorless tris(2-carboxyethyl)phosphine (TCEP) ...
The activity of PTGES2 is thought to be increased in the presence of sulfhydryl compounds, in particular dithiothreitol. The ...
4-dithiothreitol Thus, the two substrates of this enzyme are 2-methyl-3-phytyl-1,4-naphthoquinone and oxidized dithiothreitol, ... The systematic name of this enzyme class is 2-methyl-3-phytyl-1,4-naphthoquinone:oxidized-dithiothreitol oxidoreductase. This ... whereas its two products are 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone and 1,4-dithiothreitol. This enzyme ... oxidized dithiothreitol ⇌ {\displaystyle \rightleftharpoons } 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1, ...
... effects of dithiothreitol and pepstatin A". Plant & Cell Physiology. 40 (11): 1119-26. doi:10.1093/oxfordjournals.pcp.a029496. ...
Free CoA can be regenerated from CoA disulfide and mixed CoA disulfides with reducing agents such as dithiothreitol or 2- ...
The systematic name of this enzyme class is 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone:oxidized-dithi othreitol ... 4-dithiothreitol. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH or CH2 groups of ... 4-dithiothreitol Thus, the two substrates of this enzyme are 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone and oxidized ... oxidized dithiothreitol ⇌ {\displaystyle \rightleftharpoons } 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1, ...
Antifreeze protein Dithiothreitol, a thiol derivative of threitol Threitol at Sigma-Alrich https://iupac.qmul.ac.uk/2carb/19. ...
... uses a chemical called dithiothreitol (DTT) to disrupt the sulfur bonds in the protamines in order to ...
A common 1,4-dithiol is dithiothreitol (DTT), HSCH2CH(OH)CH(OH)CH2SH, sometimes called Cleland's reagent, for to reduce protein ... a vitamin Dithiothreitol, a reagent in protein biochemistry Geminal dithiols have the formula RR'C(SH)2. They are derived from ...
This can be sidelined by either pretreatment of the erythrocytes with dithiothreitol (DTT) or by using an anti-CD38 antibody ...
A molecule of DTV ((2S,3S)-1,4-Dimercaptobutane-2,3-diol), more commonly known as DTT (dithiothreitol), is also present within ...
... and the antibody is resistant to treatment with dithiothreitol.: 686 Guinea pig urine contains very high concentrations of Sd(a ...
Aerosols Air Pollutants Article Dithiothreitol Environmental Health Environmental Monitoring Humans Oxidative Stress Particle ... Size distributions of water-insoluble and water-soluble OP, (dithiothreitol assay, measure of oxidative potential per air ... Ambient Size Distributions and Lung Deposition of Aerosol Dithiothreitol-Measured Oxidative Potential: Contrast between Soluble ... Ambient Size Distributions and Lung Deposition of Aerosol Dithiothreitol-Measured Oxidative Potential: Contrast between Soluble ...
DL-1,4-DITHIOTHREITOL (D10, 98%). DLM-2622-0.5. 0.5 G. 98%. DSCD2CD(OD)CD(OD)CD2SD. 1.554,80 € ... DL-1,4-DITHIOTHREITOL (D10, 98%). DLM-2622-PK. G. 98%. DSCD2CD(OD)CD(OD)CD2SD. Request For Quote ...
Treating RBCs with dithiothreitol (DTT) eliminates the DARA interference. We conducted an international, multicenter, blinded ... International validation of a dithiothreitol (DTT)-based method to resolve the daratumumab interference with blood ... International validation of a dithiothreitol (DTT)-based method to resolve the daratumumab interference with blood ... Antibodies, Antibodies, Monoclonal, Blood Banks, Blood Safety, Dithiothreitol, Histocompatibility Testing, Humans, Methods, ...
For sputum specimens, 300 μL of the specimen was combined with 300 μL of 1,4-Dithiothreitol (12.5mM; Fisher Scientific) and ...
Lead displaces zinc from the enzyme, but this inhibition can be reversed by administering supplemental zinc or dithiothreitol. ...
... dithiothreitol (DTT) reduces homocysteine bound to albumin and to other small molecules, homocystine, and mixed disulfides, to ... dithiothreitol (DTT) reduces homocysteine bound to albumin and to other small molecules, homocysteine, and mixed disulfides, to ... serum or a whole blood hemolysate sample with 125I-folate and 57Co-vitamin B12 in a solution containing dithiothreitol (DTT) ...
4-dithiothreitol (DTT; Cat# 6908.2) from Carl Roth, iodoacetamide (IAA; Bioultra; Cat# I1149) and urea (puriss. P.a., reag. Ph ...
1863021; Bio-Rad), 2.2 μl reverse transcriptase, 1.1 μl dithiothreitol (DTT), and primers and probes at a final concentration ...
Samples were reduced by the addition of 1 mM dithiothreitol and alkylated under a nitrogen atmosphere with 10 mM iodoacetamide ...
1 mmdithiothreitol (DTT), and 0.3 mm PMSF (three times for 30 sec each; Branson sonifier; output control, 4). Membrane pellets ...
... dithiothreitol (DTT) and 0.5% (v/v) ampholytes (40% BioLyte® 3/10 Ampholyte, Bio-Rad Laboratories, Inc., Hercules, CA, USA) to ...
Disulfide groups can be converted to SH groups by reducing agents such as dithiothreitol (DTT) or β mercaptoethanol. Then, SH- ...
Changes in the concentration of Mg2+ and dithiothreitol had little or no effect on the enzymatic activity of AGPase. It has ... Changes in the concentration of Mg2+ and dithiothreitol had little or no effect on the enzymatic activity of AGPase. It has ...
1 mM dithiothreitol, 0.5 mM phenylmethylsulfonyl fluoride) along with a phosphatase inhibitor mixture (78,420; Thermo ...
Dithiothreitol greatly stimulated the enzyme activity, maximum stimulation being observed at more than 5 mm-dithiothreitol. ...
Dive into the research topics of Activation of NFκB and MnSOD gene expression by free radical scavengers in human microvascular endothelial cells. Together they form a unique fingerprint. ...
Intestinal epithelial cells were isolated by sequential incubation of intestinal tissue in pre-heated 1 mM dithiothreitol and ...
0.03 mM dithiothreitol, protease inhibitor cocktail). The suspension was taken through 5-6 cycles of freeze-thaw to ensure ...
1 M dithiothreitol (DTT; Roth 6908.3). *200 mM iodoacetamide (Sigma I1149); prepare fresh directly before use and keep in the ...
... dithiothreitol; EBSS: Earles Balanced Salt Solution; EGFP: enhanced green fluorescent protein; EIF2S1/eIF2α: eukaryotic ...
DTT: Dithiothreitol. EDTA: Ethylenediaminetetraacetic acid. IAA: Iodoacetamide. IPTG: Isopropyl β-D-1-thiogalactopyranoside ...
DT-Dithiothreitol; Promega), 4 U/μL RNasin Plus RNase inhibitor (Promega), and 0.64 μM Igepal (Sigma) in RNase free water ( ...
  • Disulfide groups can be converted to SH groups by reducing agents such as dithiothreitol (DTT) or β mercaptoethanol. (dojindo.com)
  • We show that nontoxic concentrations of the thiol-capping reagent (Ellman's reagent) or thiol-reducing agent (dithiothreitol) effectively inhibit the time-dependent development of adhesive spore strength after attachment to a surface. (uhi.ac.uk)
  • Dithiothreitol (DTT) is used in proteomics applications to maintain sulfhydryl (-SH) groups in the reduced state and for quantitative reduction of disulfide (-S-S-) groups. (sigmaaldrich.com)
  • We have developed an assay for PM redox activity, utilizing the reduction of oxygen by dithiothreitol which serves as an electron source. (cdc.gov)
  • Dithiothreitol is an effective reducing agent for protein analysis. (sigmaaldrich.com)
  • The S-S reducing agent, dithiothreitol (DTT) altered the properties of nicotinic receptors in rat superior cervical ganglia such that (i) carbachol became less active as a depolarizing agent and (ii) bromo- acetylcholine produced an irreversible depolarization. (ox.ac.uk)
  • Dithiothreitol greatly stimulated the enzyme activity, maximum stimulation being observed at more than 5 m m -dithiothreitol. (microbiologyresearch.org)
  • The cellular and recombinant species of modified PRX3 were resistant to dithiothreitol and SDS and suppressed by NAC, indicating that TS covalently adducts cysteine residues in PRX3. (cdc.gov)