A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
Solutions prepared for exchange across a semipermeable membrane of solutes below a molecular size determined by the cutoff threshold of the membrane material.
A normal intermediate in the fermentation (oxidation, metabolism) of sugar. The concentrated form is used internally to prevent gastrointestinal fermentation. (From Stedman, 26th ed)
Inorganic salts that contain the -HCO3 radical. They are an important factor in determining the pH of the blood and the concentration of bicarbonate ions is regulated by the kidney. Levels in the blood are an index of the alkali reserve or buffering capacity.
Salts or esters of LACTIC ACID containing the general formula CH3CHOHCOOR.
Alcohol oxidoreductases with substrate specificity for LACTIC ACID.
A zinc-containing enzyme which oxidizes primary and secondary alcohols or hemiacetals in the presence of NAD. In alcoholic fermentation, it catalyzes the final step of reducing an aldehyde to an alcohol in the presence of NADH and hydrogen.
Enzymes that catalyze the dehydrogenation of GLYCERALDEHYDE 3-PHOSPHATE. Several types of glyceraldehyde-3-phosphate-dehydrogenase exist including phosphorylating and non-phosphorylating varieties and ones that transfer hydrogen to NADP and ones that transfer hydrogen to NAD.
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
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)
An enzyme that catalyzes the conversion of L-glutamate and water to 2-oxoglutarate and NH3 in the presence of NAD+. (From Enzyme Nomenclature, 1992) EC 1.4.1.2.
An enzyme that oxidizes an aldehyde in the presence of NAD+ and water to an acid and NADH. This enzyme was formerly classified as EC 1.1.1.70.
An enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle. (From Dorland, 27th ed) (The NADP+ enzyme is EC 1.1.1.42.) EC 1.1.1.41.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
Amino-substituted glyoxylic acid derivative.
A subclass of enzymes which includes all dehydrogenases acting on primary and secondary alcohols as well as hemiacetals. They are further classified according to the acceptor which can be NAD+ or NADP+ (subclass 1.1.1), cytochrome (1.1.2), oxygen (1.1.3), quinone (1.1.5), or another acceptor (1.1.99).
A flavoprotein containing oxidoreductase that catalyzes the dehydrogenation of SUCCINATE to fumarate. In most eukaryotic organisms this enzyme is a component of mitochondrial electron transport complex II.
An alcohol oxidoreductase which catalyzes the oxidation of L-iditol to L-sorbose in the presence of NAD. It also acts on D-glucitol to form D-fructose. It also acts on other closely related sugar alcohols to form the corresponding sugar. EC 1.1.1.14
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
An enzyme of the oxidoreductase class that catalyzes the reaction 6-phospho-D-gluconate and NADP+ to yield D-ribulose 5-phosphate, carbon dioxide, and NADPH. The reaction is a step in the pentose phosphate pathway of glucose metabolism. (From Dorland, 27th ed) EC 1.1.1.43.
The rate dynamics in chemical or physical systems.
A glucose dehydrogenase that catalyzes the oxidation of beta-D-glucose to form D-glucono-1,5-lactone, using NAD as well as NADP as a coenzyme.
Enzymes of the oxidoreductase class that catalyze the dehydrogenation of hydroxysteroids. (From Enzyme Nomenclature, 1992) EC 1.1.-.
Oxidoreductases that are specific for ALDEHYDES.
D-Glucose:1-oxidoreductases. Catalyzes the oxidation of D-glucose to D-glucono-gamma-lactone and reduced acceptor. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.47; EC 1.1.1.118; EC 1.1.1.119 and EC 1.1.99.10.
Catalyze the oxidation of 3-hydroxysteroids to 3-ketosteroids.
Reversibly catalyzes the oxidation of a hydroxyl group of sugar alcohols to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2. and EC 1.1.99.
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
Enzymes that catalyze the first step in the beta-oxidation of FATTY ACIDS.
A transferase that catalyzes formation of PHOSPHOCREATINE from ATP + CREATINE. The reaction stores ATP energy as phosphocreatine. Three cytoplasmic ISOENZYMES have been identified in human tissues: the MM type from SKELETAL MUSCLE, the MB type from myocardial tissue and the BB type from nervous tissue as well as a mitochondrial isoenzyme. Macro-creatine kinase refers to creatine kinase complexed with other serum proteins.
An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
Enzymes that reversibly catalyze the oxidation of a 3-hydroxyacyl CoA to 3-ketoacyl CoA in the presence of NAD. They are key enzymes in the oxidation of fatty acids and in mitochondrial fatty acid synthesis.
An intermediate compound in the metabolism of carbohydrates, proteins, and fats. In thiamine deficiency, its oxidation is retarded and it accumulates in the tissues, especially in nervous structures. (From Stedman, 26th ed)
Flavoproteins that catalyze reversibly the reduction of carbon dioxide to formate. Many compounds can act as acceptors, but the only physiologically active acceptor is NAD. The enzymes are active in the fermentation of sugars and other compounds to carbon dioxide and are the key enzymes in obtaining energy when bacteria are grown on formate as the main carbon source. They have been purified from bovine blood. EC 1.2.1.2.
A flavoprotein oxidoreductase that has specificity for medium-chain fatty acids. It forms a complex with ELECTRON TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
A class of enzymes that catalyzes the oxidation of 17-hydroxysteroids to 17-ketosteroids. EC 1.1.-.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
An enzyme that catalyzes the oxidation of XANTHINE in the presence of NAD+ to form URIC ACID and NADH. It acts also on a variety of other purines and aldehydes.
A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.
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)
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)
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
A ketone oxidoreductase that catalyzes the overall conversion of alpha-keto acids to ACYL-CoA and CO2. The enzyme requires THIAMINE DIPHOSPHATE as a cofactor. Defects in genes that code for subunits of the enzyme are a cause of MAPLE SYRUP URINE DISEASE. The enzyme was formerly classified as EC 1.2.4.3.
The E1 component of the multienzyme PYRUVATE DEHYDROGENASE COMPLEX. It is composed of 2 alpha subunits (pyruvate dehydrogenase E1 alpha subunit) and 2 beta subunits (pyruvate dehydrogenase E1 beta subunit).
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.
Oxidoreductases that are specific for KETONES.
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)
Hydroxysteroid dehydrogenases that catalyzes the reversible conversion of CORTISOL to the inactive metabolite CORTISONE. Enzymes in this class can utilize either NAD or NADP as cofactors.
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.
Enzymes of the transferase class that catalyze the conversion of L-aspartate and 2-ketoglutarate to oxaloacetate and L-glutamate. EC 2.6.1.1.
An oxidoreductase involved in pyrimidine base degradation. It catalyzes the catabolism of THYMINE; URACIL and the chemotherapeutic drug, 5-FLUOROURACIL.
An enzyme that catalyzes the oxidation of UDPglucose to UDPglucuronate in the presence of NAD+. EC 1.1.1.22.
A disease-producing enzyme deficiency subject to many variants, some of which cause a deficiency of GLUCOSE-6-PHOSPHATE DEHYDROGENASE activity in erythrocytes, leading to hemolytic anemia.
Enzyme that catalyzes the first step of the tricarboxylic acid cycle (CITRIC ACID CYCLE). It catalyzes the reaction of oxaloacetate and acetyl CoA to form citrate and coenzyme A. This enzyme was formerly listed as EC 4.1.3.7.
A metabolic process that converts GLUCOSE into two molecules of PYRUVIC ACID through a series of enzymatic reactions. Energy generated by this process is conserved in two molecules of ATP. Glycolysis is the universal catabolic pathway for glucose, free glucose, or glucose derived from complex CARBOHYDRATES, such as GLYCOGEN and STARCH.
Analyses for a specific enzyme activity, or of the level of a specific enzyme that is used to assess health and disease risk, for early detection of disease or disease prediction, diagnosis, and change in disease status.
A low-affinity 11 beta-hydroxysteroid dehydrogenase found in a variety of tissues, most notably in LIVER; LUNG; ADIPOSE TISSUE; vascular tissue; OVARY; and the CENTRAL NERVOUS SYSTEM. The enzyme acts reversibly and can use either NAD or NADP as cofactors.
An NAD-dependent enzyme that catalyzes the reversible DEAMINATION of L-ALANINE to PYRUVATE and AMMONIA. The enzyme is needed for growth when ALANINE is the sole CARBON or NITROGEN source. It may also play a role in CELL WALL synthesis because L-ALANINE is an important constituent of the PEPTIDOGLYCAN layer.
A 3-hydroxysteroid dehydrogenase which catalyzes the reversible reduction of the active androgen, DIHYDROTESTOSTERONE to 5 ALPHA-ANDROSTANE-3 ALPHA,17 BETA-DIOL. It also has activity towards other 3-alpha-hydroxysteroids and on 9-, 11- and 15- hydroxyprostaglandins. The enzyme is B-specific in reference to the orientation of reduced NAD or NADPH.
Sugar alcohol dehydrogenases that have specificity for MANNITOL. Enzymes in this category are generally classified according to their preference for a specific reducing cofactor.
A family of proteins involved in the transport of monocarboxylic acids such as LACTIC ACID and PYRUVIC ACID across cellular membranes.
Catalyzes reversibly the oxidation of hydroxyl groups of prostaglandins.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
A flavoprotein oxidoreductase that has specificity for short-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
A metalloflavoprotein enzyme involved the metabolism of VITAMIN A, this enzyme catalyzes the oxidation of RETINAL to RETINOIC ACID, using both NAD+ and FAD coenzymes. It also acts on both the 11-trans- and 13-cis-forms of RETINAL.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.
A group of enzymes that catalyze the reversible reduction-oxidation reaction of 20-hydroxysteroids, such as from a 20-ketosteroid to a 20-alpha-hydroxysteroid (EC 1.1.1.149) or to a 20-beta-hydroxysteroid (EC 1.1.1.53).
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
An high-affinity, NAD-dependent 11-beta-hydroxysteroid dehydrogenase that acts unidirectionally to catalyze the dehydrogenation of CORTISOL to CORTISONE. It is found predominantly in mineralocorticoid target tissues such as the KIDNEY; COLON; SWEAT GLANDS; and the PLACENTA. Absence of the enzyme leads to a fatal form of childhood hypertension termed, APPARENT MINERALOCORTICOID EXCESS SYNDROME.
D-Galactose:NAD(P)+ 1-oxidoreductases. Catalyzes the oxidation of D-galactose in the presence of NAD+ or NADP+ to D-galactono-gamma-lactone and NADH or NADPH. Includes EC 1.1.1.48 and EC 1.1.1.120.
A species ARTERIVIRUS, occurring in a number of transplantable mouse tumors. Infected mice have permanently elevated serum levels of lactate dehydrogenase.
ATP:pyruvate 2-O-phosphotransferase. A phosphotransferase that catalyzes reversibly the phosphorylation of pyruvate to phosphoenolpyruvate in the presence of ATP. It has four isozymes (L, R, M1, and M2). Deficiency of the enzyme results in hemolytic anemia. EC 2.7.1.40.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A flavoprotein oxidoreductase that has specificity for long-chain fatty acids. It forms a complex with ELECTRON-TRANSFERRING FLAVOPROTEINS and conveys reducing equivalents to UBIQUINONE.
Elements of limited time intervals, contributing to particular results or situations.
An enzyme that catalyzes the reduction of aspartic beta-semialdehyde to homoserine, which is the branch point in biosynthesis of methionine, lysine, threonine and leucine from aspartic acid. EC 1.1.1.3.
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.
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
A mitochondrial flavoprotein, this enzyme catalyzes the oxidation of 3-methylbutanoyl-CoA to 3-methylbut-2-enoyl-CoA using FAD as a cofactor. Defects in the enzyme, is associated with isovaleric acidemia (IVA).
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
An NAD+ dependent enzyme that catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate to 3-carboxy-4-methyl-2-oxopentanoate. It is involved in the biosynthesis of VALINE; LEUCINE; and ISOLEUCINE.
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.
Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES.
Derivatives of formic acids. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are formed with a single carbon carboxy group.
An enzyme of the lyase class that catalyzes the cleavage of fructose 1,6-biphosphate to form dihydroxyacetone phosphate and glyceraldehyde 3-phosphate. The enzyme also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. (Enzyme Nomenclature, 1992) E.C. 4.1.2.13.
(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.
An octameric enzyme belonging to the superfamily of amino acid dehydrogenases. Leucine dehydrogenase catalyzes the reversible oxidative deamination of L-LEUCINE, to 4-methyl-2-oxopentanoate (2-ketoisocaproate) and AMMONIA, with the corresponding reduction of the cofactor NAD+.
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
An enzyme that catalyzes the oxidation of 3-phosphoglycerate to 3-phosphohydroxypyruvate. It takes part in the L-SERINE biosynthesis pathway.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Small molecules that are required for the catalytic function of ENZYMES. Many VITAMINS are coenzymes.
Anaerobic degradation of GLUCOSE or other organic nutrients to gain energy in the form of ATP. End products vary depending on organisms, substrates, and enzymatic pathways. Common fermentation products include ETHANOL and LACTIC ACID.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A series of oxidative reactions in the breakdown of acetyl units derived from GLUCOSE; FATTY ACIDS; or AMINO ACIDS by means of tricarboxylic acid intermediates. The end products are CARBON DIOXIDE, water, and energy in the form of phosphate bonds.
Enzymes that catalyze the oxidation of estradiol at the 17-hydroxyl group in the presence of NAD+ or NADP+ to yield estrone and NADH or NADPH. The 17-hydroxyl group can be in the alpha- or beta-configuration. EC 1.1.1.62
Contractile tissue that produces movement in animals.
The complete absence, or (loosely) the paucity, of gaseous or dissolved elemental oxygen in a given place or environment. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
Inorganic or organic oxy acids of sulfur which contain the general formula RS2O2H.
An enzyme that plays a role in the GLUTAMATE and butanoate metabolism pathways by catalyzing the oxidation of succinate semialdehyde to SUCCINATE using NAD+ as a coenzyme. Deficiency of this enzyme, causes 4-hydroxybutyricaciduria, a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA).
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The span of viability of a cell characterized by the capacity to perform certain functions such as metabolism, growth, reproduction, some form of responsiveness, and adaptability.
A strain of albino rat developed at the Wistar Institute that has spread widely at other institutions. This has markedly diluted the original strain.
Allosteric enzymes that regulate glycolysis and gluconeogenesis. These enzymes catalyze phosphorylation of fructose-6-phosphate to either fructose-1,6-bisphosphate (PHOSPHOFRUCTOKINASE-1 reaction), or to fructose-2,6-bisphosphate (PHOSPHOFRUCTOKINASE-2 reaction).
An NAD-dependent glyceraldehyde-3-phosphate dehydrogenase found in the cytosol of eucaryotes. It catalyses the dehydrogenation and phosphorylation of GLYCERALDEHYDE 3-PHOSPHATE to 3-phospho-D-glyceroyl phosphate, which is an important step in the GLYCOLYSIS pathway.
Diphosphoric acid esters of fructose. The fructose-1,6- diphosphate isomer is most prevalent. It is an important intermediate in the glycolysis process.
The chemical reactions involved in the production and utilization of various forms of energy in cells.
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Method of analyzing chemicals using automation.
A subclass of enzymes which includes all dehydrogenases acting on carbon-carbon bonds. This enzyme group includes all the enzymes that introduce double bonds into substrates by direct dehydrogenation of carbon-carbon single bonds.
An enzyme that catalyzes the conversion of prephenate to p-hydroxyphenylpyruvate in the presence of NAD. In the enteric bacteria, this enzyme also possesses chorismate mutase activity, thereby catalyzing the first two steps in the biosynthesis of tyrosine. EC 1.3.1.12.
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
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.
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.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
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.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
An enzyme that catalyzes the conversion of ATP and a D-hexose to ADP and a D-hexose 6-phosphate. D-Glucose, D-mannose, D-fructose, sorbitol, and D-glucosamine can act as acceptors; ITP and dATP can act as donors. The liver isoenzyme has sometimes been called glucokinase. (From Enzyme Nomenclature, 1992) EC 2.7.1.1.
Life or metabolic reactions occurring in an environment containing oxygen.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
An enzyme that catalyzes the conversion of L-alanine and 2-oxoglutarate to pyruvate and L-glutamate. (From Enzyme Nomenclature, 1992) EC 2.6.1.2.
The sum of the weight of all the atoms in a molecule.
An enzyme that catalyzes the oxidation of 1-pyrroline-5-carboxylate to L-GLUTAMATE in the presence of NAD. Defects in the enzyme are the cause of hyperprolinemia II.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The 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 degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A clear, colorless liquid rapidly absorbed from the gastrointestinal tract and distributed throughout the body. It has bactericidal activity and is used often as a topical disinfectant. It is widely used as a solvent and preservative in pharmaceutical preparations as well as serving as the primary ingredient in ALCOHOLIC BEVERAGES.
A flavoprotein enzyme that is responsible for the catabolism of LYSINE; HYDROXYLYSINE; and TRYPTOPHAN. It catalyzes the oxidation of GLUTARYL-CoA to crotonoyl-CoA using FAD as a cofactor. Glutaric aciduria type I is an inborn error of metabolism due to the deficiency of glutaryl-CoA dehydrogenase.
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Biosynthesis of GLUCOSE from nonhexose or non-carbohydrate precursors, such as LACTATE; PYRUVATE; ALANINE; and GLYCEROL.
The pathological process occurring in cells that are dying from irreparable injuries. It is caused by the progressive, uncontrolled action of degradative ENZYMES, leading to MITOCHONDRIAL SWELLING, nuclear flocculation, and cell lysis. It is distinct it from APOPTOSIS, which is a normal, regulated cellular process.
Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.
An enzymes that catalyzes the reversible reduction-oxidation reaction of 20-alpha-hydroxysteroids, such as from PROGESTERONE to 20-ALPHA-DIHYDROPROGESTERONE.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
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 colorless, flammable liquid used in the manufacture of acetic acid, perfumes, and flavors. It is also an intermediate in the metabolism of alcohol. It has a general narcotic action and also causes irritation of mucous membranes. Large doses may cause death from respiratory paralysis.
Enzymes catalyzing the dehydrogenation of secondary amines, introducing a C=N double bond as the primary reaction. In some cases this is later hydrolyzed.
Derivatives of OXALIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that are derived from the ethanedioic acid structure.
Acidosis caused by accumulation of lactic acid more rapidly than it can be metabolized. It may occur spontaneously or in association with diseases such as DIABETES MELLITUS; LEUKEMIA; or LIVER FAILURE.
An electrochemical process in which macromolecules or colloidal particles with a net electric charge migrate in a solution under the influence of an electric current.
An enzyme catalyzing the transfer of a phosphate group from 3-phospho-D-glycerate in the presence of ATP to yield 3-phospho-D-glyceroyl phosphate and ADP. EC 2.7.2.3.
The relationship between the dose of an administered drug and the response of the organism to the drug.
The termination of the cell's ability to carry out vital functions such as metabolism, growth, reproduction, responsiveness, and adaptability.
Amine oxidoreductases that use either NAD+ (EC 1.5.1.7) or NADP+ (EC 1.5.1.8) as an acceptor to form L-LYSINE or NAD+ (EC 1.5.1.9) or NADP+ (EC 1.5.1.10) as an acceptor to form L-GLUTAMATE. Deficiency of this enzyme causes HYPERLYSINEMIAS.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
A non-pathogenic species of LACTOCOCCUS found in DAIRY PRODUCTS and responsible for the souring of MILK and the production of LACTIC ACID.
The phenomenon whereby compounds whose molecules have the same number and kind of atoms and the same atomic arrangement, but differ in their spatial relationships. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
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 subtype of striated muscle, attached by TENDONS to the SKELETON. Skeletal muscles are innervated and their movement can be consciously controlled. They are also called voluntary muscles.
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.
Stable carbon atoms that have the same atomic number as the element carbon, but differ in atomic weight. C-13 is a stable carbon isotope.
An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
The functional hereditary units of BACTERIA.
A prediction of the probable outcome of a disease based on a individual's condition and the usual course of the disease as seen in similar situations.
Sharks of the family Squalidae, also called dogfish sharks. They comprise at least eight genera and 44 species. Their LIVER is valued for its oil and its flesh is often made into fertilizer.
Treatment process involving the injection of fluid into an organ or tissue.
A FLAVOPROTEIN enzyme that catalyzes the oxidative demethylation of dimethylglycine to SARCOSINE and FORMALDEHYDE.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
An enzyme that catalyzes the conversion of L-aspartate 4-semialdehyde, orthophosphate, and NADP+ to yield L-4-aspartyl phosphate and NADPH. EC 1.2.1.11.
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).
A product of fermentation. It is a component of the butanediol cycle in microorganisms. In mammals it is oxidized to carbon dioxide.
Proteins found in any species of bacterium.
Lengthy and continuous deprivation of food. (Stedman, 25th ed)
An NAD+ dependent enzyme that catalyzes the oxidation of betain aldehyde to BETAINE.
Electrophoresis in which agar or agarose gel is used as the diffusion medium.
Cellular processes in biosynthesis (anabolism) and degradation (catabolism) of CARBOHYDRATES.
An examination of chemicals in the blood.
An aldotriose which is an important intermediate in glycolysis and in tryptophan biosynthesis.
Damage to the MYOCARDIUM resulting from MYOCARDIAL REPERFUSION (restoration of blood flow to ischemic areas of the HEART.) Reperfusion takes place when there is spontaneous thrombolysis, THROMBOLYTIC THERAPY, collateral flow from other coronary vascular beds, or reversal of vasospasm.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.1.
Proteins prepared by recombinant DNA technology.
An inherited metabolic disorder caused by deficient enzyme activity in the PYRUVATE DEHYDROGENASE COMPLEX, resulting in deficiency of acetyl CoA and reduced synthesis of acetylcholine. Two clinical forms are recognized: neonatal and juvenile. The neonatal form is a relatively common cause of lactic acidosis in the first weeks of life and may also feature an erythematous rash. The juvenile form presents with lactic acidosis, alopecia, intermittent ATAXIA; SEIZURES; and an erythematous rash. (From J Inherit Metab Dis 1996;19(4):452-62) Autosomal recessive and X-linked forms are caused by mutations in the genes for the three different enzyme components of this multisubunit pyruvate dehydrogenase complex. One of the mutations at Xp22.2-p22.1 in the gene for the E1 alpha component of the complex leads to LEIGH DISEASE.
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.
Electrophoresis in which a starch gel (a mixture of amylose and amylopectin) is used as the diffusion medium.
A species of GRAM-POSITIVE ENDOSPORE-FORMING BACTERIA in the family BACILLACEAE, found in soil, hot springs, Arctic waters, ocean sediments, and spoiled food products.
An aldose-ketose isomerase that catalyzes the reversible interconversion of glucose 6-phosphate and fructose 6-phosphate. In prokaryotic and eukaryotic organisms it plays an essential role in glycolytic and gluconeogenic pathways. In mammalian systems the enzyme is found in the cytoplasm and as a secreted protein. This secreted form of glucose-6-phosphate isomerase has been referred to as autocrine motility factor or neuroleukin, and acts as a cytokine which binds to the AUTOCRINE MOTILITY FACTOR RECEPTOR. Deficiency of the enzyme in humans is an autosomal recessive trait, which results in CONGENITAL NONSPHEROCYTIC HEMOLYTIC ANEMIA.
The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.
Derivatives of caproic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated six carbon aliphatic structure.
A series of steps taken in order to conduct research.
The destruction of ERYTHROCYTES by many different causal agents such as antibodies, bacteria, chemicals, temperature, and changes in tonicity.
A trihydroxy sugar alcohol that is an intermediate in carbohydrate and lipid metabolism. It is used as a solvent, emollient, pharmaceutical agent, and sweetening agent.
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
A colorless, odorless gas that can be formed by the body and is necessary for the respiration cycle of plants and animals.

Early death during chemotherapy in patients with small-cell lung cancer: derivation of a prognostic index for toxic death and progression. (1/4809)

Based on an increased frequency of early death (death within the first treatment cycle) in our two latest randomized trials of combination chemotherapy in small-cell lung cancer (SCLC), we wanted to identify patients at risk of early non-toxic death (ENTD) and early toxic death (ETD). Data were stored in a database and logistic regression analyses were performed to identify predictive factors for early death. During the first cycle, 118 out of 937 patients (12.6%) died. In 38 patients (4%), the cause of death was sepsis. Significant risk factors were age, performance status (PS), lactate dehydrogenase (LDH) and treatment with epipodophyllotoxins and platinum in the first cycle (EP). Risk factors for ENTD were age, PS and LDH. Extensive stage had a hazard ratio of 1.9 (P = 0.07). Risk factors for ETD were EP, PS and LDH, whereas age and stage were not. For EP, the hazard ratio was as high as 6.7 (P = 0.0001). We introduced a simple prognostic algorithm including performance status, LDH and age. Using a prognostic algorithm to exclude poor-risk patients from trials, we could minimize early death, improve long-term survival and increase the survival differences between different regimens. We suggest that other groups evaluate our algorithm and exclude poor prognosis patients from trials of dose intensification.  (+info)

Inhibition of doxorubicin toxicity in cultured neonatal mouse cardiomyocytes with elevated metallothionein levels. (2/4809)

Controversial results have been reported regarding whether metallothionein (MT) functions in doxorubicin (DOX) detoxification in the heart. To determine unequivocally the role of MT in cardiac protection against the toxicity of DOX, ventricular cardiomyocytes isolated from 1- to 3-day neonatal transgenic mice with high levels of cardiac MT and from nontransgenic control animals were applied. On the 6th day of culturing, MT concentrations in the transgenic cardiomyocytes were about 2-fold higher than those in the nontransgenic cells. DOX was added directly into the cultures. Compared with nontransgenic controls, transgenic cardiomyocytes displayed a significant (p <.05) resistance to DOX cytotoxicity, as measured by morphological alterations, cell viability, and lactate dehydrogenase leakage from the cells. This cytoprotective effect of MT correlated with its inhibition of DOX-induced lipid peroxidation. These observations demonstrate unequivocally that elevation of MT concentrations in the cardiomyocytes of 2-fold higher than normal provides efficient protection against DOX toxicity.  (+info)

Evolutionary analysis of TATA-less proximal promoter function. (3/4809)

Many molecular studies describe how components of the proximal promoter affect transcriptional processes. However, these studies do not account for the likely effects of distant enhancers or chromatin structure, and thus it is difficult to conclude that the sequence variation in proximal promoters acts to modulate transcription in the natural context of the whole genome. This problem, the biological importance of proximal promoter sequence variation, can be addressed using a combination of molecular and evolutionary analyses. Provided here are molecular and evolutionary analyses of the variation in promoter function and sequence within and between populations of Fundulus heteroclitus for the lactate dehydrogenase-B (Ldh-B) proximal promoter. Approximately one third of the Ldh-B proximal promoter contains interspersed regions that are functionally important: (1) they bind transcription factors in vivo, (2) they effect a change in transcription as assayed by transient transfection into two different fish cell lines, and (3) they bind purified transcription factors in vitro. Evolutionary analyses that compare sequence variation in these functional regions versus the nonfunctional regions indicate that the changes in the Ldh-B proximal promoter sequences are due to directional selection. Thus, the Ldh-B proximal promoter sequence variations that affect transcriptional processes constitute a phenotypic change that is subject to natural selection, suggesting that proximal promoter sequence variation affects transcription in the natural context of the whole genome.  (+info)

The use of variable lactate/malic dehydrogenase ratios to distinguish between progenitor cells of cartilage and bone in the embryonic chick. (4/4809)

The activities of LDH and MDH have been studied, both in differentiated cartilage and bone from the embryonic chick, and in the pool of mixed osteogenic and chondrogenic stem cells found on the quadratojugal, a membrane bone. In confirmation of the model proposed by Reddi & Huggins (1971) we found that the LDH/MDH ratio was greater than 1 in cartilage and less than 1 in bone. Furthermore we established, for the first time, that ratios occurred in the chondrogenic and osteogenic stem cells, similar to the ratios in their differentiated counterparts. Alteration in LDH/MDH resulted from variations in the level of LDH/mug protein. MDH/mug protein remained constant, even when LDH/MDH was changing. We interpret these results in terms of adaptation of chondrogenic progenitor cells for anaerobic metabolism and anticipate that our model will be applicable to other skeletal systems where stem cells are being studied.  (+info)

Enrichment of canalicular membrane with cholesterol and sphingomyelin prevents bile salt-induced hepatic damage. (5/4809)

These studies were undertaken to characterize the role of plasma membrane cholesterol in canalicular secretory functions and hepatocyte integrity against intravenous taurocholate administration. Cholesterol and sphingomyelin concentrations and cholesterol/phospholipid ratios were significantly increased in canalicular membranes of diosgenin-fed rats, suggesting a more resistant structure against solubilization by taurocholate. During taurocholate infusion, control rats had significantly decreased bile flow, whereas diosgenin-fed animals maintained bile flow. Maximal cholesterol output increased by 176% in diosgenin-fed rats, suggesting an increased precursor pool of biliary cholesterol in these animals. Maximal phospholipid output only increased by 43% in diosgenin-fed rats, whereas bile salt output remained at control levels. The kinetics of glutamic oxalacetic transaminase, lactic dehydrogenase, and alkaline phosphatase activities in bile showed a significantly faster release in control than in diosgenin-fed rats. After 30 min of intravenous taurocholate infusion, necrotic hepatocytes were significantly increased in control animals. Preservation of bile secretory functions and hepatocellular cytoprotection by diosgenin against the intravenous infusion of toxic doses of taurocholate was associated with an increased concentration of cholesterol and sphingomyelin in the canalicular membrane. The increase of biliary cholesterol output induced by diosgenin was correlated to the enhanced concentration of cholesterol in the canalicular membrane.  (+info)

Development of diving capacity in emperor penguins. (6/4809)

To compare the diving capacities of juvenile and adult emperor penguins Aptenodytes forsteri, and to determine the physiological variables underlying the diving ability of juveniles, we monitored diving activity in juvenile penguins fitted with satellite-linked time/depth recorders and examined developmental changes in body mass (Mb), hemoglobin concentration, myoglobin (Mb) content and muscle citrate synthase and lactate dehydrogenase activities. Diving depth, diving duration and time-at-depth histograms were obtained from two fledged juveniles during the first 2.5 months after their depature from the Cape Washingon colony in the Ross Sea, Antarctica. During this period, values of all three diving variables increased progressively. After 8-10 weeks at sea, 24-41 % of transmitted maximum diving depths were between 80 and 200 m. Although most dives lasted less than 2 min during the 2 month period, 8-25 % of transmitted dives in the last 2 weeks lasted 2-4 min. These values are lower than those previously recorded in adults during foraging trips. Of the physiological variables examined during chick and juvenile development, only Mb and Mb content did not approach adult values. In both near-fledge chicks and juveniles, Mb was 50-60 % of adult values and Mb content was 24-31 % of adult values. This suggests that the increase in diving capacity of juveniles at sea will be most dependent on changes in these factors.  (+info)

Protective effects of transient HO-1 overexpression on susceptibility to oxygen toxicity in lung cells. (7/4809)

Rat fetal lung cells (RFL-6) were transiently transfected with a full-length rat heme oxygenase (HO)-1 cDNA construct and then exposed to hyperoxia (95% O2-5% CO2) for 48 h. Total HO activity and HO-1 protein were measured as well as cell viability, lactate dehydrogenase (LDH) release, protein oxidation, lipid peroxidation, and total glutathione to measure oxidative injury. HO-1 overexpression resulted in increased total HO activity (2-fold), increased HO-1 protein (1.5-fold), and increased cell proliferation. Immunohistochemistry revealed perinuclear HO-1 localization, followed by migration to the nucleus by day 3. Decreased cell death, protein oxidation, and lipid peroxidation but increased LDH release and glutathione depletion were seen with HO-1 overexpression. Reactive iron content could not explain the apparent loss of cell membrane integrity. With the addition of tin mesoporphyrin, total HO activity was decreased and all changes in injury parameters were normalized to control values. We conclude that moderate overexpression of HO-1 is protective against oxidative injury, but we speculate that there is a beneficial threshold of HO-1 expression.  (+info)

Comparison of a parasite lactate dehydrogenase-based immunochromatographic antigen detection assay (OptiMAL) with microscopy for the detection of malaria parasites in human blood samples. (8/4809)

Microscopic examination of blood smears remains the gold standard for malaria diagnosis, but is labor-intensive and requires skilled operators. Rapid dipstick technology provides a potential alternative. A study was conducted in The Gambia to compare the performance of OptiMAL, an immunochromatographic antigen detection assay for the diagnosis of malaria using parasite lactate dehydrogenase, against standard microscopy in patients with suspected malaria. For initial diagnosis of Plasmodium falciparum, irrespective of stage, this assay had a sensitivity of 91.3%, a specificity of 92%, a positive predictive value of 87.2%, and a negative predictive value of 94.7%. The sensitivity of the test decreased markedly at parasitemias < 0.01%. This assay can be used for the diagnosis of malaria in areas where microscopy is not available and for urgent malaria diagnosis at night and at weekends, when routine laboratories are closed and when relatively inexperienced microscopists may be on duty.  (+info)

definition of HLDH5, what does HLDH5 mean?, meaning of HLDH5, Human Lactate Dehydrogenase Isoenzyme 5, HLDH5 stands for Human Lactate Dehydrogenase Isoenzyme 5
The lactate dehydrogenase isoenzyme pattern of human lymphocitic cells has been determined in several people before and after stimulation by mitogenic lectins at different times after the start of the culture. A very significant change take place in the LDH 5 which can reach a greater concentration towards the other isoenzymes at the 72 h from the mitogenic stimulus, even if it starts from a smaller concentration.
Total lactate dehydrogenase (LDH; EC 1.1.1.27) activity and the percentage distribution of LDH isoenzymes were determined in 127 patients with malignant diseases. A shift in the isoenzyme patterns was observed toward the M-type, with an increase in the percentage of LDH-4 and LDH-5 isoenzymes and a slight increase in total LDH activity of all patients. Serum samples from 68 of the patients contained an abnormal isoenzyme of LDH, LDH-1 ex, that, on agarose gel electrophoresis at pH 8.6, migrated between albumin and LDH-1 isoenzyme. Chemotherapy, radiotherapy, or surgical removal of the tumor was accompanied by disappearance of this abnormal isoenzyme. The heat stability of LDH-1 ex isoenzyme appears to be similar to that of LDH-1 but greater than that of the other LDH isoenzymes. Statistical analysis of these data demonstrated a significant correlation between malignancy and the appearance of LDH-1 ex isoenzyme (P less than 0.001). In contrast, the relationship between LDH-1 ex isoenzyme and metastasis
TY - JOUR. T1 - Evaluation of peritoneal fluid pH, glucose concentration, and lactate dehydrogenase activity for detection of septic peritonitis in horses. AU - Van Hoogmoed, Linda. AU - Rodger, Lynn D.. AU - Spier, Sharon. AU - Gardner, Ian. AU - Yarbrough, Tom B.. AU - Snyder, Jack R.. PY - 1999/4/1. Y1 - 1999/4/1. N2 - Objective - To determine whether peritoneal fluid pH, glucose concentration, and lactate dehydrogenase activity can be used to differentiate horses with septic peritonitis from those with nonseptic peritonitis. Design - Prospective study. Animals - 46 horses, including 10 healthy horses, 15 horses with septic peritonitis, and 21 horses with nonseptic peritonitis. Procedure - Peritoneal fluid and blood samples were analyzed for pH, glucose concentration, and lactate dehydrogenase activity. Complete blood cell counts were performed, and peritoneal fluid samples were submitted for bacterial culture. Results - Horses with septic peritonitis had significantly lower peritoneal fluid ...
Buy our Recombinant human Lactate Dehydrogenase B protein. Ab96765 is an active full length protein produced in Escherichia coli and has been validated in…
TY - JOUR. T1 - Structure of Toxoplasma gondii LDH1. T2 - Active-Site Differences from Human Lactate Dehydrogenases and the Structural Basis for Efficient APAD+ Use. AU - Kavanagh, Kathryn L.. AU - Elling, Robert A.. AU - Wilson, David K.. PY - 2004/2/3. Y1 - 2004/2/3. N2 - While within a human host the opportunistic pathogen Toxoplasma gondii relies heavily on glycolysis for its energy needs. Lactate dehydrogenase (LDH), the terminal enzyme in anaerobic glycolysis necessary for NAD+ regeneration, therefore represents an attractive therapeutic target. The tachyzoite stage lactate dehydrogenase (LDH1) from the parasite T. gondii has been crystallized in apo form and in ternary complexes containing NAD + or the NAD+-analogue 3-acetylpyridine adenine dinucleotide (APAD+) and sulfate or the inhibitor oxalate. Comparison of the apo and ternary models shows an active-site loop that becomes ordered upon substrate binding. This active-site loop is five residues longer than in most LDHs and necessarily ...
In rare cases, a mutation in the genes controlling the production of lactate dehydrogenase will lead to a medical condition known as lactate dehydrogenase deficiency. Depending on which gene carries the mutation, one of two types will occur: either lactate dehydrogenase-A deficiency (also known as glycogen storage disease XI) or lactate dehydrogenase-B deficiency. Both of these conditions affect how the body breaks down sugars, primarily in certain muscle cells. Lactate dehydrogenase-A deficiency is caused by a mutation to the LDHA gene, while lactate dehydrogenase-B deficiency is caused by a mutation to the LDHB gene.[10]. This condition is inherited in an autosomal recessive pattern, meaning that both parents must contribute a mutated gene in order for this condition to be expressed.[11]. A complete lactate dehydrogenase enzyme consists of four protein subunits.[12] Since the two most common subunits found in lactate dehydrogenase are encoded by the LDHA and LDHB genes, either variation of ...
7.6. typical examples of protein-separating gel electrophoresis at skeleton. Lactate Dehydrogenase delightful to be able to the web site, in this time Ill show you in relation to Lactate dehydrogenase.. And after this, this can be a very first impression, lactate dehydrogenase, lactate dehydrogenase test, lactate dehydrogenase molecular weight, lactate dehydrogenase high, lactate dehydrogenase deficiency, lactate dehydrogenase function, lactate dehydrogenase normal range, lactate dehydrogenase levels, lactate dehydrogenase assay, lactate dehydrogenase (ldh) :. ...
Lactate, the anion that results from dissociation of lactic acid, is an intracellular metabolite of glucose; specifically it is the end product of anaerobic glycolysis, the final step of which is conversion of pyruvate to lactate by the enzyme lactate dehydrogenase. The two lactate isomers are known as L-lactate and D-lactate. Both forms (stereoisomers) of lactate are produced from and metabolized to pyruvate by the action of the enzyme lactate dehydrogenase (LDH). However, the enzyme is isomer-specific so that production and metabolism of D-lactate requires D-LDH and L-lactate requires L-LDH. Mammalian cells only contain L-LDH so that in humans the lactate produced is almost exclusively L-lactate. Carbohydrate-fermenting bacterial species (e.g. Lactobacillus spp) have by contrast both enzymes and therefore the capacity to produce both D-lactate and L-lactate. Some species produce only D-lactate, some only L-lactate and others both forms.. L-lactate is thus normally present in human body. If ...
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Lactate dehydrogenase (LDH) isoenzymes are required for adenosine triphosphate production, with each of five different isoenzymes having varying proficiencies in anaerobic versus aerobic environments. With advancing pregnancy, the isoenzyme profile in uterine muscle shifts toward a more anaerobic profile, speculatively to facilitate uterine efficiency during periods of low oxygen that accompany labor contractions. Profile shifting may even occur throughout labor. Maternal serum LDH levels between 24-48 hours following delivery predominantly originate from uterine muscle, reflecting the enzymatic state of the myometrium during labor. Our purpose was to describe serum LDH isoenzymes 24-30 hours post-delivery to determine if cervical dilation rates following labor admission were associated with a particular LDH profile. We also compared differences in post-delivery LDH isoenzyme profiles between women admitted in pre-active versus established active labor. Low-risk, nulliparous women with spontaneous labor
The aim of many in vitro models of acute or chronic degenerative disorders in the neurobiology field is the assessment of survival or damage of neuronal cells. Damage of cells is associated with loss of outer cell membrane integrity and leakage of cytoplasmic cellular proteins. Therefore, activity assays of cytoplasmic enzymes in supernatants of cell cultures serve as a practicable tool for quantification of cellular injury (Koh and Choi, 1987; Bruer et al., 1997). Lactate dehydrogenase (LDH) is such a ubiquitously expressed cytosolic enzyme, which is very stable due to a very long protein half-life (Hsieh and Blumenthal, 1956; Koh and Cotman, 1992; Koh et al., 1995)., 神经生物学领域中许多急性或慢性退行性疾病的体外模型的目的是评估神经元细胞的存活或损伤。细胞损伤与外细胞膜完整性的丧失和细胞质细胞蛋白的泄漏有关。因此,细胞培养上清液中细胞质酶的活性测定作为细胞损伤定量的实用工具(Koh和Choi,1987;
Lymphocytes. Lactic dehydrogenase isoenzymes. Total LDH is actually a group of enzymes. The individual enzymes (isoenzymes) that make up total LDH have different concentrations in different tissues. Therefore, the tissue responsible for an elevated total LDH value may often be identified by fractionation (separation) and measurement of individual isoenzymes. In addition, since the population normal range for total LDH is rather wide, abnormal elevation of one isoenzyme may occur without lifting total LDH out of the total LDH normal range.. Five main fractions (isoenzymes) of LDH are measured. With use of the standard international nomenclature (early U.S. investigators used opposite terminology), fraction 1 is found mainly in RBCs and in heart and kidney, fraction 3 comes from lung, and fraction 5 is located predominantly in liver and to a lesser extent in skeletal muscle. Skeletal muscle contains some percentage of all the fractions, although fraction 5 predominates. Various methods of ...
The Worldwide Lactate Dehydrogenase Test Market is expected to reach $ 6.4 billion by the end of 2023; this market is projecsted to growing at a CAGR of ~ 8.8 % during 2017-2023. The Global Lactate Dehydrogenase Test Market report has been segmented as lactate dehydrogenase 1 (LD1), lactate dehydrogenase 2 (LD2), lactate dehydrogenase 3 (LD3), lactate dehydrogenase 4 (LD4), and lactate dehydrogenase 5 (LD5).. The Global Lactate Dehydrogenase Test Market report explores the major key Players in-depth analysis as LifeSpan BioSciences, Aviva Systems Biology, Accurex Biomedical Pvt. Ltd., Thermo Fisher Scientific, Bioo Scientific Corporation, Quest Diagnostics, Abcam plc., Randox Laboratories Ltd., Sigma-Aldrich Co. LLC., Merck KGaA and others.. Get Sample Copy @ https://www.marketresearchfuture.com/sample_request/3884 .. The faster market uptake of new technology in the US is also an important driver of the market for global lactate dehydrogenase test. Lactate dehydrogenase (LDH) is an enzyme ...
Most cancer cells use aerobic glycolysis to fuel their growth. The enzyme lactate dehydrogenase-A (LDH-A) is key to cancers glycolytic phenotype, catalysing the regeneration of nicotinamide adenine dinucleotide (NAD þ ) from reduced nicotinamide adenine dinucleotide (NADH) necessary to sustain glycolysis. As such, LDH-A is a promising target for anticancer therapy. Here we ask if the tumour suppressor p53, a major regulator of cellular metabolism, influences the response of cancer cells to LDH-A suppression. LDH-A knockdown by RNA interference (RNAi) induced cancer cell death in p53 wild-type, mutant and p53-null human cancer cell lines, indicating that endogenous LDH-A promotes cancer cell survival irrespective of cancer cell p53 status. Unexpectedly,however,weuncoveredanovelroleforp53intheregulationofcancercellNADþ anditsreducedformNADH.Thus, LDH-A silencing by RNAi, or its inhibition using a small-molecule inhibitor, resulted in a p53-dependent increase in the cancer cell ...
The present study was designed to obtain an experimental tumor model as similar as possible to human ovarian cancer which often had a large amount of ascites and to assess the therapeutic value of tranexamic acid. Human tumor cell lines which form ascites in nude mice were established from ascites of patient with serous cystadenocarcinoma of the ovary. Two cloned cell lines designated HRA and HR-1 were obtained from the parent cell line designated HR. All of these cultured cell lines had about 2.5-3.5 times higher lactate dehydrogenase activities than the original tumor. The original tumor and the tumor grown in nude mice had all 5 bands of lactate dehydrogenase isoenzymes, while all cultured cell lines had only a marked lactate dehydrogenase-3 in addition to a faint lactate dehydrogenase-2. Modal chromosome numbers of HR cells ranged from 50-76, while that of HRA cells ranged widely from 40-140. The DNA histograms of HR and HRA cells were similar to each other, showing predominant G1 and S ...
Molecular Cloning, also known as Maniatis, has served as the foundation of technical expertise in labs worldwide for 30 years. No other manual has been so popular, or so influential.
Abstract: Antigenic properties of human, pig, rabbit and rat lactate dehydrogenase (LDH) M4-isozyme as well as of human LDH-C4 were studied using antipeptide antibodies against pig LDH-M4 fragment (180-214). Amino acid sequence 180-214, containing His-195, which is involved in the active site of LDH isozymes, proved to be total antigenic determinant only for human and pig M4-isozymes. Amino acid sequence of total antigenic determinant did not allow any substitutions of essential amino acid residues. His-195, participating in substrate binding, was not involved immediately in reactions with antibodies as shown by means of chemical modification of pig M4-isozyme with diethyl pyrocarbonate and after production of antibodies against the modified isoenzyme ...
Nonspecific elevation of levels of transaminase or lactic acid dehydrogenase [LDH] information including symptoms, causes, diseases, symptoms, treatments, and other medical and health issues.
Eppley PW, Rutherford J. Bacterial meningitis in childhood: lactic acid dehydrogenase in cerebrospinal fluid. J Am Osteopath Assoc 1976;75(5):500. doi: .. Download citation file:. ...
This graph shows the total number of publications written about L-Lactate Dehydrogenase by people in Harvard Catalyst Profiles by year, and whether L-Lactate Dehydrogenase was a major or minor topic of these publication ...
Background: There is evidence that high level of serum lactate dehydrogenase (LDH) is associated with poorer overall survival in several malignancies, but its link to cancer-specific survival is unclear. Methods: A total of 7895 individuals diagnosed with cancer between 1986 and 1999 were selected for this study. Multivariable Cox proportional hazards regression was used to assess overall and cancer-specific death by the z-score and clinical categories of serum LDH prospectively collected within 3 years before diagnosis. Site-specific analysis was performed for major cancers. Analysis was repeated by different lag times between LDH measurements and diagnosis. Results: At the end of follow-up, 5799 participants were deceased. Hazard ratios (HRs) and 95% confidence intervals (CIs) for overall and cancer-specific death in the multivariable model were 1.43 (1.31-1.56) and 1.46 (1.32-1.61), respectively, for high compared with low prediagnostic LDH. Site-specific analysis showed high LDH to correlate ...
|b||i|Background:|/i||/b| Lactate dehydrogenase 5 (LDH5) is a major lactate dehydrogenase isoenzyme catalyzing the transformation of pyruvate to lactate to provide anaerobic en
The oxygen-regulated control system responsible for the induction of erythropoietin (Epo) by hypoxia is present in most (if not all) cells and operates on other genes, including those involved in energy metabolism. To understand the organization of cis-acting sequences that are responsible for oxygen-regulated gene expression, we have studied the 5 flanking region of the mouse gene encoding the hypoxically inducible enzyme lactate dehydrogenase A (LDH). Deletional and mutational analysis of the function of mouse LDH-reporter fusion gene constructs in transient transfection assays defined three domains, between -41 and -84 base pairs upstream of the transcription initiation site, which were crucial for oxygen-regulated expression. The most important of these, although not capable of driving hypoxic induction in isolation, had the consensus of a hypoxia-inducible factor 1 (HIF-1) site, and cross-competed for the binding of HIF-1 with functionally active Epo and phosphoglycerate kinase-1 sequences. The
Biochemical characterization and kinetic analysis of epsilon-crystallin from the lenses of common ducks were undertaken to elucidate the enzyme mechanism of this unique crystallin with lactate dehydrogenase (LDH) activity. Despite the structural similarities between epsilon-crystallin and chicken heart LDH, differences in charge and kinetic properties were revealed by isoenzyme electrophoresis and kinetic studies. Bi-substrate kinetic analysis examined by initial-velocity and product-inhibition studies suggested a compulsory ordered Bi Bi sequential mechanism with NADH as the leading substrate followed by pyruvate. The products were released in the order L-lactate and NAD+. The catalysed reaction is shown to have a higher rate in the formation of L-lactate and NAD+. Substrate inhibition was observed at high concentrations of pyruvate and L-lactate for the forward and reverse reactions respectively. The substrate inhibition was presumably due to the formation of epsilon-crystallin-NAD(+)-pyruvate ...
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This test measures different enzymes in your blood. You may need this test if youve had a heart attack, or if you have a blood disorder or liver damage.
Anti-Lactate Dehydrogenase Isoenzyme V antibody (ab9002) has been cited in 20 publications. References for Human, Mouse in IHC, IHC-Fr, IHC-P, WB
Lactate Dehyderogenase, Serum (LDH): View interpretation of results, purpose, procedure, answers to patient concerns/FAQs and book at lowest prices from labs and diagnostic centers in your city on 1mg.com.
The increase in LC3 flux and LLPD after Rab7b knockdown, together with the increase in size of LC3‐positive vesicles, suggests that sequestration of content into autophagosomes should also be increased. To investigate this, we measured the transfer of the autophagic cargo marker enzyme lactate dehydrogenase (LDH) from the cytosol to autophagosomes [36]. In this assay, BafA1 is added to prevent autolysosomal degradation of LDH, thus allowing the assessment of autophagic sequestration activity per se, instead of the net effect of autophagic sequestration and degradation.. Rab7b depletion led to a significant increase in LDH sequestration under starvation conditions, as well as after treatment with Torin1 (more than 1.5‐fold increase and twofold increase respectively; Fig 4E). Expression of HA‐Rab7b after Rab7b silencing significantly reversed the effect of Rab7b depletion on LDH sequestration, demonstrating the specificity of the Rab7b siRNA (Fig 4E). Of note, we observed a tendency of ...
Coronavirus disease 2019 pandemic causes significant strain on healthcare infrastructure and medical resources. So, it becomes crucial to identify reliable predictor biomarkers for COVID-19 disease severity and short term mortality. Many biomarkers are currently investigated for their prognostic role in COVID-19 patients. Our study is retrospective and aims to evaluate role of semi-quantitative CT-severity scoring versus LDH as prognostic biomarkers for COVID-19 disease severity and short-term clinical outcome. Two hundred sixty-six patients between April 2020 and November 2020 with positive RT-PCR results underwent non-enhanced CT scan chest in our hospital and were retrospectively evaluated for CT severity scoring and serum LDH level measurement. Data were correlated with clinical disease severity. CT severity score and LDH were significantly higher in severe and critical cases compared to mild cases (P value | 0.001). High predictive significance of CT severity score for COVID-19 disease course noted
article{c3ac9f80-11f8-4d66-9522-8c076ab60131, abstract = {Purpose: This trial of the German High-Grade Non-Hodgkins Lymphoma Study Group compares the use of high-dose therapy (HDT) as part of primary treatment with cyclophosphamide, doxorubicin, vincristine, and prednisone (CHOP) plus etoposide followed by involved-field (IF) radiotherapy in a randomized, multicenter, phase III study. Patients and Methods: Three hundred twelve patients with aggressive non-Hodgkins lymphoma aged greater than or equal to 60 years with elevated serum lactate dehydrogenase levels were included from 1990 to 1997. Patients with at least a minor response after two cycles of CHOEP (CHOP + etoposide 3 x 100 mg/m(2)) were to receive three further cycles of CHOEP followed by IF radiotherapy (arm A) or one further cycle of CHOEP followed by autologous stem-cell transplantation and IF radiotherapy (arm B). Results: Among 158 patients randomized to arm B, 103 (65%) received HDT. The complete remission rate at the end of ...
The break down of glucose to provide energy, through coupled reactions to resythesise ADP back into ATP.. Glucose is supplied directly from carbs or glycogen. the carbohydrated is located in the liver and muscles and are a ready fuel source.. a decrease in PC activates the enyzme glycogen phosphorylase to break down glycogen during the process glycolysis.. takes place in the sarcoplasm of muscle cells and is anaerobic.. during glycolysis the enzyme phosphoructokinase (PFK) initiates the breakdown of glucose into pyruvic acid but if there is a lack of oxygen, pyruvic acid is turned into lactic acid by the enzyme lactate dehydrogenase.. provides energy during the first 2-3mins of high intensity short duration work. if the activity is flat out the la system may only last up to 30secs. ...
Types of Anaerobic Respiration. Which route the cells take to create the ATP depends solely on whether or not there is enough oxygen present to undergo aerobic respiration. This reaction is catalyzed by the enzyme lactate dehydrogenase. So, if youre going to become a brewer, make sure you do your homework! After glycolysis, both the aerobic and anaerobic cells send the two pyruvate molecules through a series of chemical reactions to generate more ATP and extract electrons for use in their electron transport chain. Many other organisms can perform either aerobic or anaerobic respiration, depending on whether oxygen is present. As such, fermentation produces two ATP molecules, which are further used to split a glucose molecule into two three-carbon atom chains. This medium contains a range of oxygen concentrations, producing a gradient. Plants can also respire anaerobically. Anaerobic respiration refers to the type of respiration that takes place in the absence of oxygen. Aerobic respiration, ...
Total Lactate Dehydrogenase (LD):. LD activity is present in all cells of the body with highest concentrations in heart, liver, muscle, kidney, lung, and erythrocytes. As with other proteins used as tissue-function markers, the appearance of LD in the serum occurs only after prolonged hypoxia and is elevated in a number of clinical conditions including cardiorespiratory diseases, malignancy, hemolysis, and disorders of the liver, kidneys, lung, and muscle.. Isoenzymes:. LD is a tetrameric cytoplasmic enzyme, composed of H and M subunits. The usual designation of the isoenzyme is LD-I (H4), LD-II (H3M), LD-III (H2M2), LD-IV (HM3), and LD-V (M4). Tissue specificity is derived from the fact that tissue-specific synthesis of subunits occurs in well-defined ratios. Most notably, heart muscle cells preferentially synthesize H subunits, while liver cells synthesize M subunits nearly exclusively. Skeletal muscle also synthesizes largely M subunits so that LD-V is both a liver and skeletal muscle form of ...
MICROBIAL CELL FACTORIES. L-lactic acid production from D-xylose with Candida sonorensis expressing a heterologous lactate dehydrogenase encoding gene. Kari T Koivuranta1*, Marja Ilmén1, Marilyn G Wiebe1, Laura Ruohonen1, Pirkko Suominen2 and Merja Penttilä1. Background: Bioplastics, like polylactic acid (PLA), are renewable alternatives for petroleum-based plastics. Lactic acid, the monomer of PLA, has traditionally been produced biotechnologically with bacteria. With genetic engineering, yeast have the potential to replace bacteria in biotechnological lactic acid production, with the benefits of being acid tolerant and having simple nutritional requirements. Lactate dehydrogenase genes have been introduced to various yeast to demonstrate this potential. Importantly, an industrial lactic acid producing process utilising yeast has already been implemented. Utilisation of D-xylose in addition to D-glucose in production of biochemicals such as lactic acid by microbial fermentation would be ...
casSAR Dugability of B4SMK1 | lldD | L-lactate dehydrogenase - Also known as LLDD_STRM5, lldD. Catalyzes the conversion of L-lactate to pyruvate. Is coupled to the respiratory chain.
1. The very fast pre-steady-state formation of NADH catalysed by pig M4 lactate dehydrogenase was equivalent to the enzyme-site concentration at pH values greater than 8.0 and to one-half the site concentration at pH6.8. 2. The rate of dissociation of NADH from the enzyme at pH8.0 (450s−1) in the absence of other substrates is faster than the steady-state oxidation of lactate (80s−1). The latter process is therefore controlled by a step before NADH dissociation but subsequent to the hydride transfer. 3. The oxidation of enzyme-NADH by excess of pyruvate was studied as a first-order process at pH9.0. There was no effect of NADD on this reaction and it was concluded that the ternary complex undergoes a rate-limiting change before the hydride-transfer step. 4. Some conclusions about the reactions catalysed by the M4 isoenzyme were drawn from a comparison of these results with those obtained with the H4 isoenzyme and liver alcohol dehydrogenase.. ...
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LACTATE DEHYDROGENASE (LD). 1-30 days: 135-750 U/L. 31 days-11 months: 180-435 U/L. 1-3 years: 160-370 U/L. 4-6 years: 145-345 U/L. 7-9 years: 143-290 U/L. 10-12 years: 120-293 U/L. 13-15 years: 110-283 U/L. 16-17 years: 105-233 U/L. ≥18 years: 122-222 U/L. LD ISOENZYMES. I (fast band): 17.5-28.3%. II: 30.4-36.4%. III: 19.2-24.8%. IV: 9.6-15.6%. V (slow band): 5.5-12.7%. ...
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HBD has been used as a substitute for LDH-1 (heart) isoenzyme measurement. Actually, HBD is total LDH that is forced to act on a a-ketobutyric acid substrate instead of pyruvic or lactic acid. Under these conditions, LDH-1 and LDH-2 show relatively greater activity than LDH-5, so that HBD therefore indirectly measures LDH-1 (heart) activity. However, if the LDH-5 (liver) value is elevated sufficiently, it will also produce measurable HBD effect. Therefore, HBD is not as specific as electrophoresis or heat fractionation in separating heart from liver isoenzymes. Nevertheless, since HBD assay is easier to perform (and therefore cheaper) than LDH isoenzyme assay, some follow the practice of using a more specific isoenzyme method if in doubt about LDH heart versus liver contribution. Once there is proof that the heart fraction is elevated, they follow subsequent activity levels with HBD.. Causes of lactic dehydrogenase fraction 1 elevation ...
An enzyme that is found in almost all of the bodys cells, but only a small amount of it is usually detectable in the blood. LDH is released from the cells into the bloodstream when cells are damaged or destroyed. Because of this, the LDH test can be used as a general marker of injury to cells.. ...
The Motzer score (high/poor risk, intermediate risk, low risk) is based on the number of the following poor prognostic features a participant possessed: ECOG ,2, serum lactate dehydrogenase concentration , 1.5 times the upper limit of normal, hemoglobin , lower limit of normal, corrected calcium concentration , 10 mg/dl, and absence of prior nephrectomy. Participants who had none of these features = low risk; participants with 1 or 2 of these features = intermediate risk; participants with 3 or more of these features = high/poor risk and were excluded from participating in the study ...
Discusses test to help diagnose lung disease, lymphoma, anemia, liver disease, and also to see how well chemotherapy is working during treatment for lymphoma. Looks at possible results.
Background: Hypermethylation of DNA is an epigenetic alteration commonly found in colorectal cancer (CRC) and can also be detected in blood samples of cancer patients. Methylation of the genes helicase-like transcription factor (HLTF) and hyperplastic polyposis 1 (HPP1) have been proposed as prognostic, and neurogenin 1 (NEUROG1) as diagnostic biomarker. However the underlying mechanisms leading to the release of these genes are unclear. This study aimed at examining the possible correlation of the presence of methylated genes NEUROG1, HLTF and HPP1 in serum with tissue breakdown as a possible mechanism using serum lactate dehydrogenase (LDH) as a surrogate marker. Additionally the prognostic impact of these markers was examined. Methods: Pretherapeutic serum samples from 259 patients from all cancer stages were analyzed. Presence of hypermethylation of the genes HLTF, HPP1, and NEUROG1 was examined using methylation-specific quantitative PCR (MethyLight). LDH was determined using an UV kinetic ...
Lactate dehydrogenase (also called lactic acid dehydrogenase, or LDH) is an enzyme found in almost all body tissues. The LDH test is generally used to screen for tissue damage.
Elevated LDH was associated with poor prognosis in patients with COVID-19, indicating 37% posterior probability for composite poor outcome with AUC of 0.77, sensitivity of 74%, and specificity of 69%.. The incidence of LDH was associated with presence of diabetes, this phenomenon might be due to reduced glycogen synthesis, change in glucose oxidative metabolism and elevated whole-body rate of non-oxidative glycolysis.28-31 These mechanisms cause elevated lactate in patients with insulin resistance compared with those without. LDH has been found to affect the prognosis of various diseases, including cancers.32 LDH elevation in patients with COVID-19 indicates lung and tissue injuries.19 COVID-19 may lead to inadequate tissue perfusion and multiple organ failure due to various mechanisms, including thrombosis, which lead to LDH elevation.2 33 Thus, high LDH serves as a biomarker of the disease extent. This study indicated that the association between LDH elevation and poor prognosis was not ...
from lactate (Cori cycle):. *Lactate dehydrogenase. from alanine (Alanine cycle):. *Alanine transaminase ...
from lactate (Cori cycle):. *Lactate dehydrogenase. from alanine (Alanine cycle):. *Alanine transaminase ... lactate metabolic process. • glycolytic process. • phosphorylation. • fructose metabolic process. • response to glucose. • ...
S-(hydroxymethyl)glutathion dehydrogenase Ja 1.1.1.300 NADP-retinol dehydrogenase Ja 1.1.2.4 D-lactate dehydrogenase ( ... oxoglutarate dehydrogenase (succinyl-transferring) Ja 1.2.4.4 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl- ... L-iditol 2-dehydrogenase Ja 1.1.1.15 D-iditol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. D-sorbose + NADH + H+ D-iditol 2- ... D-arabitol 4-dehydrogenase 1.1.1.12 L-arabitol + NAD+ ⇌. {\displaystyle \rightleftharpoons }. L-xylulose + NADH + H+ L-arabitol ...
P. falciparum lactate dehydrogenase (PfLDH) is a 33 kDa oxidoreductase [EC 1.1.1.27].[14] It is the last enzyme of the ... Bzik DJ, Fox BA, Gonyer K (1993). "Expression of Plasmodium falciparum lactate dehydrogenase in Escherichia coli". Mol Biochem ... Vander Jagt DL, Hunsaker LA, Heidrich JE (1981). "Partial purification and characterization of lactate dehydrogenase from ... Parasite Lactate Dehydrogenase, and Panmalarial Antigen Reactivity after Clearance of Plasmodium falciparum Monoinfection". J ...
One study examined the sperm-specific isozyme of human lactate dehydrogenase (LDH-C4) combined with a T-cell epitope to create ... Goldberg, E (1990). "Developmental expression of lactate dehydrogenase isozymes during spermatogenesis". Prog Clin Biol Res. ... "Immunization of female cynomolgus macaques with a synthetic epitope of sperm-specific lactate dehyrogenase results in high ...
Lactic acid fermentation converts pyruvate to lactate by lactate dehydrogenase. Most importantly, fermentation regenerates NAD+ ... The buildup of lactate and its substrates for lactate production, pyruvate and alanine, lead to excess lactate.[9] Normally, ... Instead of accumulating inside the muscle cells, lactate produced by anaerobic fermentation is taken up by the liver. This ... From an intuitive perspective, gluconeogenesis reverses both glycolysis and fermentation by converting lactate first into ...
Lactate formation is catalyzed by lactate dehydrogenase in a reversible reaction. Lactate can also be used as an indirect ... Pyruvate is oxidized to acetyl-CoA and CO2 by the pyruvate dehydrogenase complex (PDC). The PDC contains multiple copies of ... During recovery, when oxygen becomes available, NAD+ attaches to hydrogen from lactate to form ATP. In yeast, the waste ... In humans, aerobic conditions produce pyruvate and anaerobic conditions produce lactate. In aerobic conditions, the process ...
Biellmann JF, Lapinte C, Haid E, Weimann G (1979). "Structure of lactate dehydrogenase inhibitor generated from coenzyme". ... Lesk AM (1995). "NAD-binding domains of dehydrogenases". Curr. Opin. Struct. Biol. 5 (6): 775-83. doi:10.1016/0959-440X(95) ... Jameson DM, Thomas V, Zhou DM (1989). "Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase ...
Biellmann JF, Lapinte C, Haid E, Weimann G (1979). "Structure of lactate dehydrogenase inhibitor generated from coenzyme". ... Lesk AM (1995). "NAD-binding domains of dehydrogenases". Curr. Opin. Struct. Biol. 5 (6): 775-83. PMID 8749365. doi:10.1016/ ... Jameson DM, Thomas V, Zhou DM (1989). "Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase ... Franchetti P, Grifantini M (1999). "Nucleoside and non-nucleoside IMP dehydrogenase inhibitors as antitumor and antiviral ...
Rossmann fold in part of the lactate dehydrogenase of Cryptosporidium parvum, showing NAD+ in red, beta sheets in yellow, and ... Biellmann JF, Lapinte C, Haid E, Weimann G (1979). "Structure of lactate dehydrogenase inhibitor generated from coenzyme". ... including glyceraldehyde 3-phosphate dehydrogenase and pyruvate dehydrogenase. In healthy mammalian tissues, estimates of the ... Lesk AM (1995). "NAD-binding domains of dehydrogenases". Curr. Opin. Struct. Biol. 5 (6): 775-83. doi:10.1016/0959-440X(95) ...
"Structure and function of lactate dehydrogenase from hagfish". Marine Drugs. 8 (3): 594-607. doi:10.3390/md8030594. PMC 2857353 ...
Biellmann JF, Lapinte C, Haid E, Weimann G «Structure of lactate dehydrogenase inhibitor generated from coenzyme». Biochemistry ... Lesk AM «NAD-binding domains of dehydrogenases». Curr. Opin. Struct. Biol., 5, 6, 1995, pàg. 775-83. DOI: 10.1016/0959-440X(95) ... Jameson DM, Thomas V, Zhou DM «Time-resolved fluorescence studies on NADH bound to mitochondrial malate dehydrogenase». Biochim ... Franchetti P, Grifantini M «Nucleoside and non-nucleoside IMP dehydrogenase inhibitors as antitumor and antiviral agents». Curr ...
In this situation, lactate dehydrogenase levels increase and gas exchange is compromised. Oxygen is less able to diffuse into ...
Blood investigations include lactate dehydrogenase (LDH), serum uric acid, and kidney function tests.[42] ...
எ.கா: பல உயிரினங்களிலும் செடிகொடியினங்களிலும் காணப்படும் லாக்டேட் டிஐதரோச்செனேசு (Lactate dehydrogenase) (1.1.1.27) ... எ.கா: 1.1.1.1 என்பது ஆல்க்ககால் டிஐதரோச்செனேசு (Alcohol dehydrogenase) குடும்ப நொதிகளைக் குறிக்கும் நொதிஎண் ஆகும். ...
The enzyme lactate dehydrogenase is made of two (H-form and M-Form) different sub units, combines in different combinations ... for example lactate dehydrogenase (LDH)). In biochemistry, isozymes (or isoenzymes) are isoforms (closely related variants) of ...
In this study, we assayed the cell viability, the percentage of lactate dehydrogenase released (% LDH released), the level of ...
"Evaluation of a new Plasmodium lactate dehydrogenase assay (OptiMAL-IT) for the detection of malaria". Transact Royal Soc Trop ... 1986). "Antibodies to the glutamate dehydrogenase of Plasmodium falciparum". Parasitology 92,: 313-24. doi:10.1017/ ...
Patients who have a hemoglobin level of less than 12 g/dL, a lactate dehydrogenase level higher than normal, and/or a blood ...
... elevated lactate dehydrogenase (LDH, a chemical released from damaged cells, and which is therefore a marker of cellular damage ...
... lactate dehydrogenase) isoenzyme complex composition and decreases the activity of the lactate generating enzyme LDHA, while ... Strength training is typically associated with the production of lactate, which is a limiting factor of exercise performance. ... Regular endurance exercise leads to adaptations in skeletal muscle which can prevent lactate levels from rising during strength ... lactate, that creates the "burn" feeling in the muscle, resulting in that the muscle tissue can tolerate higher stress for a ...
... rise in lactate dehydrogenase (LDH), positive direct antiglobulin test (DAT), positive crossmatch" [27] This is due to ...
Elevated lactate dehydrogenase (LDH) levels. No standardized protocol exist regarding the management of LVAD pump thrombosis. ... The unexpected abrupt increase in LVAD thrombosis was accompanied by elevated lactate dehydrogenase (LDH) levels with outcomes ... Elevation of lactate dehydrogenase during the first month offers an opportunity for early intervention strategies. Starting in ...
16 mmol/litre Lactate dehydrogenase (LDH) > 600iu/litre Aspartate transaminase (AST) > 200iu/litre Albumin < 32g/litre Glucose ... 16 mmol/litre Enzymes lactate dehydrogenase (LDH) > 600iu/litre aspartate transaminase (AST) > 200iu/litre Albumin < 32g/litre ...
Reduction by lactate dehydrogenase produces lactate. Pyruvate is sold as a weight-loss supplement, though credible science has ... from glycolysis is converted by fermentation to lactate using the enzyme lactate dehydrogenase and the coenzyme NADH in lactate ... If insufficient oxygen is available, the acid is broken down anaerobically, creating lactate in animals and ethanol in plants ... Jaimes, R., III (Jul 2015). "Functional response of the isolated, perfused normoxic heart to pyruvate dehydrogenase activation ...
... enzyme lactate dehydrogenase)--> L-lactate + NAD Blood sugar MBAS assay, an assay that indicates anionic surfactants in water ...
Lactate dehydrogenase (LDH) is found in many body tissues, including the liver. Elevated levels of LDH may indicate liver ... "How Often Should You Check Your Liver Function?". "Lactate Dehydrogenase (LDH) Test: MedlinePlus Medical Test". medlineplus.gov ... Those babies with Rh hemolytic disease, ABO incompatibility with the mother, Glucose-6-phosphate dehydrogenase (G-6-PD) ...
Muscle enzymes are increased, commonly lactate dehydrogenase (LDH). Many dietary factors and aberrations can induce ANIM. ... and lactate dehydrogenase are closely examined. Abnormal levels of these proteins are indicative of both inflammatory myopathy ... Patients with a glycogen storage disease manifest a normal increase in ammonia but no change from baseline of lactate, whereas ... During vigorous ischemic exercise, skeletal muscle functions aerobically, generating lactate and ammonia a coproduct of muscle ...
Nishiguchi, Y.; Ito, I.; Okada, M. (2010). "Structure and function of lactate dehydrogenase from hagfish". Marine Drugs. 8 (3 ...
... is a possible pyruvate analog that has the ability to halt lactate production by inhibiting lactate dehydrogenase, ... effectively stopping the conversation process of pyruvate to lactate. Oxamate [lactate dehydrogenase (LDH) inhibitor] plus ... Oxamate is a competitive inhibitor of the enzyme lactate dehydrogenase. ... Due to the inherent ability of Oxamate to prevent the conversion of pyruvate to lactate, oxamate can be used to counter balance ...
Pervasive and required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ... male or female neither pregnant nor lactating ...
D-lactate dehydrogenase (cytochrome). *D-lactate dehydrogenase (cytochrome c-553). *Mannitol dehydrogenase (cytochrome) ...
l-galactonolactone dehydrogenase.[131] to produce ascorbic acid.[122] l-Ascorbic acid has a negative feedback on l-galactose ... and for pregnant and lactating women.[3] For the European Union, the EFSA set higher recommendations for adults, and also for ... l-galactose dehydrogenase, whereby the lactone ring opens and forms again but with between the carbonyl on C1 and hydroxyl ... UDP-glucose 6-dehydrogenase uses the co-factor NAD+ as the electron acceptor. The transferase UDP-glucuronate pyrophosphorylase ...
A classical or pure seminoma by definition do not cause an elevated serum alpha fetoprotein .[6] Lactate dehydrogenase (LDH) ...
UDP-glucose 6-dehydrogenase uses the co-factor NAD+ as the electron acceptor. The transferase UDP-glucuronate pyrophosphorylase ... and for pregnant and lactating women.[3] For the European Union, the EFSA set higher recommendations for adults, and also for ... Leferink, N. G.; van den Berg, W. A.; van Berkel, W. J. (2008). "L-Galactono-γ-lactone Dehydrogenase from Arabidopsis thaliana ... L-Galactose reacts with the enzyme L-galactose dehydrogenase, whereby the lactone ring opens and forms again but with between ...
D-lactate dehydrogenase (cytochrome). *D-lactate dehydrogenase (cytochrome c-553). *Mannitol dehydrogenase (cytochrome) ... Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, ... In enzymology, a homoisocitrate dehydrogenase (EC 1.1.1.87) is an enzyme that catalyzes the chemical reaction ... Rowley B, Tucci AF (1970). "Homoisocitric dehydrogenase from yeast". Arch. Biochem. Biophys. 141 (2): 499-, 510. doi:10.1016/ ...
Furthermore, alcohol dehydrogenase is present in the stomach lining. After absorption, the alcohol passes to the liver through ... Mascord, D; Smith, J; Starmer, GA; Whitfield, JB (1991). "The effect of fructose on alcohol metabolism and on the [lactate]/[ ... Alcohol is metabolized mainly by the group of six enzymes collectively called alcohol dehydrogenase. These convert the ethanol ... Rate of detoxification of alcohol can also be slowed by certain drugs which interfere with the action of alcohol dehydrogenases ...
D-lactate dehydrogenase (cytochrome). *D-lactate dehydrogenase (cytochrome c-553). *Mannitol dehydrogenase (cytochrome) ... alcohol dehydrogenase (NADP+) activity. • retinal dehydrogenase activity. • allyl-alcohol dehydrogenase activity. • NADP- ... retinol dehydrogenase activity. Cellular component. • mast cell granule. • Schwann cell microvillus. • Schmidt-Lanterman ...
... lactate dehydrogenase and amino transferase values. Dengue fever was suspected but ruled out on investigation. Malarial ...
... pyruvate is either converted into alanine via alanine aminotransferase or converted into lactic acid by lactate dehydrogenase; ... Excess lactate may be seen in the urine, cerebrospinal fluid, and blood of a person with Leigh syndrome.[5] ... Thiamine (vitamin B1) may be given if pyruvate dehydrogenase deficiency is known or suspected. The symptoms of lactic acidosis ... Leigh syndrome can also be caused by deficiency of the pyruvate dehydrogenase complex (PDHC), most commonly involving a PDHC ...
... role of the lactate/pyruvate and NAD/NADH ratios". The Journal of Laboratory and Clinical Medicine. 118 (2): 146-52. PMID ... glucose-6-phosphate dehydrogenase deficiency, phosphate depletion, iron deficiency and Wilson's disease. Eryptosis can be ... see glucose-6-phosphate dehydrogenase deficiency for more. ...
... showed that jet injectors would frequently transmit the viral infection lactate dehydrogenase elevating virus (LDV) from one ...
For example, some people (predominantly East Asians) have a mutation in their alcohol dehydrogenase gene that makes this enzyme ... lactate, ketone bodies, cortisol, and glucose in blood and urine samples.[3] ... After being ingested, the ethanol in alcoholic beverages is first converted to acetaldehyde by the enzyme alcohol dehydrogenase ... In addition, about half of all East Asians convert acetaldehyde to acetic acid more slowly (via acetaldehyde dehydrogenase), ...
Lactate dehydrogenase deficiency type A. *Lactate dehydrogenase deficiency type B. *Lactate dehydrogenase deficiency type C ...
... dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on cytochrome c: D-lactate dehydrogenase ( ... lactate dehydrogenase A. (subunit M). Human lactate dehydrogenase M4 (the isoenzyme found in skeletal muscle). From PDB: 1I10​. ... D-lactate dehydrogenase, membrane binding. crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory ... Lactate dehydrogenase-A deficiency is caused by a mutation to the LDHA gene, while lactate dehydrogenase-B deficiency is caused ...
pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase (also called α-ketoglutarate dehydrogenase). *branched-chain α-keto ... Women who are pregnant or lactating require more thiamine. For pregnant and lactating women, the consequences of thiamine ... The enzymes transketolase, pyruvate dehydrogenase (PDH), and 2-oxoglutarate dehydrogenase (OGDH) are all important in ... For lactating women, thiamine is delivered in breast milk even if it results in thiamine deficiency in the mother.[15] Pregnant ...
Zinc required for several enzymes such as carboxypeptidase, liver alcohol dehydrogenase, and carbonic anhydrase ... breastfeeding women require an additional 700 mL/day above the recommended intake values for non-lactating women. Dehydration ...
"Evaluation of a new Plasmodium lactate dehydrogenase assay (OptiMAL-IT) for the detection of malaria". Transact Royal Soc Trop ... 1986). "Antibodies to the glutamate dehydrogenase of Plasmodium falciparum". Parasitology. 92, : 313-24. doi:10.1017/ ...
Lactate dehydrogenase. *Myoglobin. *Glycogen phosphorylase isoenzyme BB. Liver function tests. *Proteins *Human serum albumin ...
... namely acyl-CoA dehydrogenase, enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and thiolase. The cycle produces a new ... adipose tissue and lactating mammary glands, where the fatty acids are combined with glycerol to form triglycerides, the major ... The oxidative conversion of pyruvate into acetyl-CoA is referred to as the pyruvate dehydrogenase reaction. It is catalyzed by ... Acetyl-CoA serves as an allosteric regulator of pyruvate dehydrogenase kinase (PDK). It regulates through the ratio of acetyl- ...
... and from other parts of metabolism they include lactate from the Cori cycle. Under conditions of prolonged fasting, acetone ... This pathway is regulated through changes in the activity of glucose-6-phosphate dehydrogenase.[9] ...
ACC1 is found in the cytoplasm of all cells but is enriched in lipogenic tissue, such as adipose tissue and lactating mammary ...
D-lactate dehydrogenase (cytochrome). *D-lactate dehydrogenase (cytochrome c-553). *Mannitol dehydrogenase (cytochrome) ... In enzymology, a carnitine 3-dehydrogenase (EC 1.1.1.108) is an enzyme that catalyzes the chemical reaction ... carnitine+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH) ... "Kinetic studies of the reaction mechanism of carnitine dehydrogenase of Pseudomonas aeruginosa]. Eur. J. Biochem. (in German). ...
Lactate dehydrogenase Pyruvate / Lactate −0.19 D-amino acid dehydrogenase 2-oxoacid + ammonia / D-amino acid ? ... Competitive inhibitors of succinate dehydrogenase (complex II).[91]. Antimycin A Piscicide Complex III Binds to the Qi site of ... NADH-coenzyme Q oxidoreductase, also known as NADH dehydrogenase or complex I, is the first protein in the electron transport ... Identification of a new 2-methyl branched chain acyl-CoA dehydrogenase". J. Biol. Chem. 258 (2): 1066-76. PMID 6401712. ...
... dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on cytochrome c: D-lactate dehydrogenase ( ... lactate dehydrogenase A. (subunit M). Human lactate dehydrogenase M4 (the isoenzyme found in skeletal muscle). From PDB: 1I10​. ... D-lactate dehydrogenase, membrane binding. crystal structure of d-lactate dehydrogenase, a peripheral membrane respiratory ... Lactate dehydrogenase-A deficiency is caused by a mutation to the LDHA gene, while lactate dehydrogenase-B deficiency is caused ...
... and lactate dehydrogenase-B deficiency.People with lactate dehydrogenase-A deficiency experience fatigue, muscle pain, and ... In some people with lactate dehydrogenase-A deficiency, high-intensity exercise or other strenuous activity leads to the ... lactate dehydrogenase-A deficiency (sometimes called glycogen storage disease XI) ... Lactate dehydrogenase deficiency is a condition that affects how the body breaks down sugar to use as energy in cells, ...
... also called lactic acid dehydrogenase, or LDH) is an enzyme found in almost all body tissues. The LDH test is generally used to ... Lactate dehydrogenase (also called lactic acid dehydrogenase, or LDH) is an enzyme found in almost all body tissues. It plays ...
Lactate dehydrogenase B is a protein that in humans is encoded by the LDHB gene. This gene encodes the B subunit of lactate ... Zha X, Wang F, Wang Y, He S, Jing Y, Wu X, Zhang H (2011). "Lactate dehydrogenase B is critical for hyperactive mTOR-mediated ... "Entrez Gene: Lactate dehydrogenase B". Retrieved 2017-10-01. Philibert RA, Nelson JJ, Sandhu HK, Crowe RR, Coryell WH (2003). " ... Kim JH, Kim EL, Lee YK, Park CB, Kim BW, Wang HJ, Yoon CH, Lee SJ, Yoon G (2011). "Decreased lactate dehydrogenase B expression ...
L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in ... Lactate/malate dehydrogenase, C-terminal (IPR022383). Short name: Lactate/malate_DH_C ... L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. L-2-hydroxyisocaproate dehydrogenases ... Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase.. Proteins 43 175-85 2001 ...
Identification of Lactate Dehydrogenase Isoenzymes by Rapid Kinetics Message Subject (Your Name) has sent you a message from ... Identification of Lactate Dehydrogenase Isoenzymes by Rapid Kinetics. Michael J. Bishop, Johannes Everse, and Nathan O. Kaplan ... Stopped-flow kinetics indicate that human and chicken heart-type4 lactate dehydrogenases (LDH) become inhibited as DPNH is ...
A diagnostic test indicator for the determination of the concentration of lactate dehydrogenase in sera comprising a bibulous ... in admixture with an alkali lactate salt such as lithium lactate, sodium lactate, potassium lactate and the like, comprises the ... It can therefore be seen that once the serum is added to the test indicator, the lactate dehydrogenase therein causes a ... Available tests for the detection of the concentration of lactate dehydrogenase in body fluids have, until now, consisted of ...
Centrifuge and separate to remove cellular material. It is better to not refrigerate or freeze the specimen, but to hold at room temperature (15-25°C), with analysis done ASAP ...
Markert, C.L., and Faulhaber, I. (1965). Lactate dehydrogenase isozyme patterns of fish. J. Exp. Zool. 159: 319-332.PubMed ... Whitt, G.S. (1970). Developmental genetics of the lactate dehydrogenase isozymes of fish. J. Exp. Zool. 175: 1-35.PubMed ... Outer Segment Photoreceptor Cell Visual Pigment Visual Cycle Enzyme Lactate Dehydrogenase These keywords were added by machine ... Whitt G.S. (1975) A Unique Lactate Dehydrogenase Isozyme in the Teleost Retina. In: Ali M.A. (eds) Vision in Fishes. NATO ...
... A Identifiers Symbol LDHA Entrez 3939 HUGO 6535 OMIM 150000 RefSeq NM_005566 ... Lactate dehydrogenase - 3-Hydroxyacyl CoA dehydrogenase - Malate dehydrogenase - Isocitrate dehydrogenase - Phosphogluconate ... Pyruvate carboxylase - Phosphoenolpyruvate carboxykinase - from lactate (Cori cycle): Lactate dehydrogenase - from alanine ( ... Carbohydrate dehydrogenases - Alcohol dehydrogenase - Glycerol-3-phosphate dehydrogenase - L-xylulose reductase - Aldose ...
Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal (IPR015955). Short name: Lactate_DH/Glyco_Ohase_4_C ... L-lactate dehydrogenases are metabolic enzymes that catalyse the conversion of L-lactate to pyruvate, the last step in ... L-lactate dehydrogenase is also found as a lens crystallin in bird and crocodile eyes. Malate dehydrogenases catalyse the ... This entry represents a structural motif found at the C-terminal of lactate dehydrogenase (EC:1.1.1.27)and malate ...
IPR001557, L-lactate/malate_DH. IPR022383, Lactate/malate_DH_C. IPR001236, Lactate/malate_DH_N. IPR015955, Lactate_DH/Glyco ... IPR001557, L-lactate/malate_DH. IPR022383, Lactate/malate_DH_C. IPR001236, Lactate/malate_DH_N. IPR015955, Lactate_DH/Glyco ... "The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design.". Dunn C., ... "The structure of lactate dehydrogenase from Plasmodium falciparum reveals a new target for anti-malarial design.". Dunn C., ...
A unique form of lactate dehydrogenase was observed in the starch-gel electrophoretic patterns of adult human testes. It was ... chromatographic characteristics on diethylaminoethyl cellulose were intermediate to those observed for lactate dehydrogenase ...
L-lactate dehydrogenase. Details. Name. L-lactate dehydrogenase. Kind. protein. Organism. Plasmodium falciparum (isolate CDC / ... L-lactate dehydrogenase. Q27743. Details. Drug Relations. Drug Relations. DrugBank ID. Name. Drug group. Pharmacological action ...
ID:1,Note:Reference Interval has been last updated on 22 Apr 2013. ,Date:2013-04-29T10:35:00.000Z,Deleted:false,IsNew:true ...
Lactate dehydrogenase (LDH) is a stable cytoplasmic enzyme that is ... ... Lactate dehydrogenase (LDH) is a stable cytoplasmic enzyme that is found in all cells. LDH is rapidly released into the cell ... LDH activity can be easily quantified by using the NADH produced during the conversion of lactate to pyruvate to reduce a ...
Active Native human Lactate Dehydrogenase protein is a Native Full length protein and validated in FuncS. ab77865 content by ... Native human Lactate Dehydrogenase protein. See all Lactate Dehydrogenase proteins and peptides. ... Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. ... One unit will catalyze the transformation of one micromole of L-lactate to pyruvate per minute at 37°C and pH 8.55. ...
Buy our Recombinant human Lactate Dehydrogenase B protein. Ab96765 is an active full length protein produced in Escherichia ... Recombinant human Lactate Dehydrogenase B protein. See all Lactate Dehydrogenase B proteins and peptides. ... Note=Defects in LDHB result in deficiency of lactate dehydrogenase, a condition with no clear symptomatic consequences. Lactate ... Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. ...
... resulting in augmented blood levels of d-lactate, a stereoisomer of l-lactate, which is normally present in human blood in ... that gout can be caused by a mutation in LDHD within the putative catalytic site of the encoded d-lactate dehydrogenase, ... We showed that LDHD expression is enriched in tissues with a high metabolic rate and abundant mitochondria and that d-lactate ... In line with the human phenotype, injection of d-lactate into naive mice resulted in hyperuricemia. Thus, hyperuricemia and ...
Many cancer cells produce ATP through high-level lactic acid fermentation catalyzed by lactate dehydrogenase (LDH), which ... Lactate dehydrogenase (LDH) is an enzyme with a tetrameric structure that catalyzes pyruvate conversion to lactate and vice ... Le, A. et al. Inhibition of lactate dehydrogenase A induces oxidative stress and inhibits tumor progression. Proc. Natl. Acad. ... Synthesis and initial screening of lactate dehydrogenase inhibitor activity of 1,3-benzodioxole derivatives. *Dicky Annas1. na1 ...
L-lactate dehydrogenase (Ldhb), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha) ... L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldhc), L-lactate dehydrogenase (Ldha) ... L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase B chain (Ldhb), L-lactate dehydrogenase ... L-lactate dehydrogenase (Ldhal6b), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase (Ldha), L-lactate dehydrogenase A ...
... Am J Physiol Lung Cell Mol Physiol. 2015 Oct ... the hypothesis that ionizing radiation leads to excessive lactate production via expression of the enzyme lactate dehydrogenase ... Recently, we reported that lactate activates latent TGF-β through a pH-dependent mechanism. Here, we wanted to test ... We propose a profibrotic feed forward loop, in which radiation induces LDHA expression and lactate production, which can lead ...
lactate dehydrogenase A. (subunit M). File:Lactate dehydrogenase M4 (muscle) 1I10.png. Human lactate dehydrogenase M4 (the ... lactate dehydrogenase B. (subunit H). File:Lactate Dehydrogenase B.png. Crystal structure of B-lactate dehydrogenase. From PDB ... dependent L-lactate dehydrogenase. Other LDHs act on D-lactate and/or are dependent on cytochrome c: D-lactate dehydrogenase ( ... D-lactate dehydrogenase, membrane binding. File:PDB 1f0x EBI.jpg. crystal structure of d-lactate dehydrogenase, a peripheral ...
Lactate dehydrogenase from the hyperthermophilic bacterium thermotoga maritima: the crystal structure at 2.1 A resolution ... Description: L-LACTATE DEHYDROGENASE protein , Length: 319 No structure alignment results are available for 1A5Z.A explicitly. ...
... Daisuke Ekuni,1 Mayu Yamane- ... The aim of this study was to determine the usefulness of a new kit that can evaluate salivary lactate dehydrogenase (LD) level ... V. Alonso De La Peña, P. Diz Dios, and R. Tojo Sierra, "Relationship between lactate dehydrogenase activity in saliva and oral ... R. M. Nagler, S. Lischinsky, E. Diamond, I. Klein, and A. Z. Reznick, "New insights into salivary lactate dehydrogenase of ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
L-lactate dehydrogenase A chain. Details. Name. L-lactate dehydrogenase A chain. Kind. protein. Organism. Humans. Polypeptides ... L-lactate dehydrogenase A chain. P00338. Details. Drug Relations. Drug Relations. DrugBank ID. Name. Drug group. ...
Lactate Dehydrogenase (LDH): Biochemistry, Function and Clinical Significance. Reshma Rani. Amity Institute of Biotechnology, ... Chapter 1. Lactate Dehydrogenase Enzyme: An Old Enzyme but New Viable Target Offers New Hope in Cancer Therapeutics. (Vinit ... Chapter 2. Lactate Dehydrogenase: The Role in the Warburg Effect and Cancer. (Nazia Nazam, Ravi Teja Chavata and Pallavi ... Chapter 3. Lactate Dehydrogenase, Its Isoforms, and Its Catalytic Functions. (Aditi Dhawan and Kajal Kanchan, School of ...
Browse our Lactate Dehydrogenase A/LDHA Protein catalog backed by our Guarantee+. ... Lactate Dehydrogenase A/LDHA Proteins available through Novus Biologicals. ... Lactate Dehydrogenase A/LDHA Proteins. We offer Lactate Dehydrogenase A/LDHA Peptides and Lactate Dehydrogenase A/LDHA Proteins ... L-lactate dehydrogenase A chain protein, lactate dehydrogenase A protein, lactate dehydrogenase M protein, LDH muscle subunit ...
  • There has therefore existed, for a substantial period of time, the need for a simple testing mechanism for the determination of the concentration of serum lactate dehydrogenase in body fluids, especially the blood, which long-felt need is satisfied by the instant invention more fully discussed hereinbelow. (freepatentsonline.com)
  • Increased serum lactate dehydrogenase isoenzymes in Ph-negative chronic myeloproliferative diseases: a metabolic adaptation? (wikipedia.org)
  • Molecular and immunological associations of elevated serum lactate dehydrogenase in metastatic melanoma patients: A fresh look at an old biomarker. (harvard.edu)
  • Suitable for the detection of L(+)-Lactate in biological samples such as serum, plasma, cells, culture and fermentation media. (sigmaaldrich.com)
  • Results of the recently published meta-analyses evaluating the prognostic value of serum lactate dehydrogenase in different solid tumors. (degruyter.com)
  • Numerous studies have generated promising but incomplete evidence for the prognostic value of pretreatment serum levels of lactate dehydrogenase (S-LDH) in nasopharyngeal carcinoma (NPC). (dovepress.com)
  • This study aimed at examining the possible correlation of the presence of methylated genes NEUROG1, HLTF and HPP1 in serum with tissue breakdown as a possible mechanism using serum lactate dehydrogenase (LDH) as a surrogate marker. (uni-muenchen.de)
  • Assay: Lactate Dehydrogenase in Mouse Serum (Pubmed). (bioassaysys.com)
  • Assay: Lactate Dehydrogenase in Rat Serum, brain , intestine (Pubmed). (bioassaysys.com)
  • The aim of the present study was to examine the effect of alveolar milk ejection on l-lactate, lactate dehydrogenase (LDH), serum albumin (SA) and immunoglobulin G (IgG) compared with SCC, a commonly used indicator of mastitis. (uzh.ch)
  • Serum lactate dehydrogenase (LDH) concentrations correlate with tumor progression and poor outcome. (pubmedcentralcanada.ca)
  • To analyze the prognostic value of pre-treatment serum lactate dehydrogenase (SLDH) level in patients with nasopharyngeal carcinoma (NPC) receiving intensity-modulated radiotherapy (IMRT) with or without chemotherapy. (jcancer.org)
  • Mutations in the LDHA gene cause lactate dehydrogenase-A deficiency, and mutations in the LDHB gene cause lactate dehydrogenase-B deficiency. (medlineplus.gov)
  • Mutations in the LDHA gene result in the production of an abnormal lactate dehydrogenase-A subunit that cannot attach (bind) to other subunits to form the lactate dehydrogenase enzyme. (medlineplus.gov)
  • Optimization of 5-(2,6-dichlorophenyl)-3-hydroxy-2-mercaptocyclohex-2-enone using structure-based design strategies resulted in inhibitors with considerable improvement in biochemical potency against human lactate dehydrogenase A (LDHA). (rcsb.org)
  • These potent inhibitors were typically selective for LDHA over LDHB isoform (4-10 fold) and other structurally related malate dehydrogenases, MDH1 and MDH2 (>500 fold). (rcsb.org)
  • These compounds include 1,3-benzodioxole derivatives, such as Machilin A (Fig. 1 ), which are efficient competitive inhibitors that function by blocking the nicotinamide adenine dinucleotide (NAD) binding site of LDHA, suppressing lactate production and cancer cell growth 16 . (nature.com)
  • Here, we wanted to test the hypothesis that ionizing radiation leads to excessive lactate production via expression of the enzyme lactate dehydrogenase-A (LDHA) to promote myofibroblast differentiation. (nih.gov)
  • We demonstrate that ionizing radiation induces LDHA, lactate production, and extracellular acidification in primary human lung fibroblasts in a dose-dependent manner. (nih.gov)
  • We propose a profibrotic feed forward loop, in which radiation induces LDHA expression and lactate production, which can lead to further activation of TGF-β to drive the fibrotic process. (nih.gov)
  • We offer Lactate Dehydrogenase A/LDHA Peptides and Lactate Dehydrogenase A/LDHA Proteins for use in common research applications: ELISA, Functional, Protein Array, SDS-Page, Western Blot. (novusbio.com)
  • Each Lactate Dehydrogenase A/LDHA Peptide and Lactate Dehydrogenase A/LDHA Protein is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • Our Lactate Dehydrogenase A/LDHA Peptides and Lactate Dehydrogenase A/LDHA Proteins can be used in a variety of model species: Human, Rat. (novusbio.com)
  • Choose from our Lactate Dehydrogenase A/LDHA Peptides and Proteins. (novusbio.com)
  • We investigated the intracellular metabolic fluxes of protein kinase CK2-activating (Cα OE) cells and role of lactate dehydrogenase A (LDHA) as a contributor of tumorigenesis after reprogrammed glucose metabolism. (nature.com)
  • It was reported that high LDHA expression in human lung carcinoma and hepatocellular carcinoma markedly increased the invasive potential and was associated with the generation of lactate 11 , 12 . (nature.com)
  • The high expression of metabolic enzymes, including glutaminase (GA) and lactate dehydrogenase A (LDHA), which contribute to bioenergetics and biosynthesis of mammalian cells, has been identified in a variety of cancer types. (spandidos-publications.com)
  • Lactate dehydrogenase ( LDH ) is an enzyme ( EC 1.1.1.27) present in a wide variety of organisms, including plants and animals. (bionity.com)
  • This entry represents a structural motif found at the C-terminal of lactate dehydrogenase ( EC:1.1.1.27 )and malate dehydrogenases ( EC:1.1.1.37 ), as well as at the C-terminal of family 4 glycoside hydrolases ( EC:3.2.1 ). (ebi.ac.uk)
  • L-Lactate dehydrogenase (L-LDH, EC 1.1.1.27) is involved in the interconversion of pyruvate and L(-)-lactate, which allows the aerobic metabolism of lactate accumulated by anaerobic glycolysis following periods of exposure to lowered environmental oxygen tension, or hypoxia [ 5 ]. (biomedcentral.com)
  • LDHB gene mutations lead to the production of an abnormal lactate dehydrogenase-B subunit that cannot form the lactate dehydrogenase enzyme. (medlineplus.gov)
  • Lactate dehydrogenase B is a protein that in humans is encoded by the LDHB gene. (wikipedia.org)
  • Note=Defects in LDHB result in deficiency of lactate dehydrogenase, a condition with no clear symptomatic consequences. (abcam.com)
  • This protein is involved in step 1 of the subpathway that synthesizes (S)-lactate from pyruvate. (uniprot.org)
  • Specificity of human Lactate Dehydrogenase C antibody verified on a Protein Array containing target protein plus 383 other non-specific proteins. (novusbio.com)
  • Here we report the cloning and characterization of another novel lactate dehydrogenase gene, named as LDHAL6A (lactate dehydrogenase A-like 6A), which encodes a 332-amino-acid protein. (sigmaaldrich.com)
  • Furthermore, we found that the recombinant protein GST-LDHAL6A can catalyze the pyruvate convert into the lactate with NADH as its coenzyme. (sigmaaldrich.com)
  • Assay: Lactate Dehydrogenase in Schistosoma japonicum protein extract (Pubmed). (bioassaysys.com)
  • Lactate dehydrogenase (LDH) is a protein that helps produce energy in the body. (adam.com)
  • Disulfide bonds were found to link the nonglycosylated envelope protein VP-2/M (19 kDa), encoded by open reading frame 6, and the major envelope glycoprotein VP-3 (25 to 42 kDa), encoded by open reading frame 5, of lactate dehydrogenase-elevating virus (LDV). (asm.org)
  • Lactate dehydrogenase C is required for the protein expression of a sperm-specific isoform of lactate dehydrogenase A. (researchmap.jp)
  • It was concluded that in most cases, analysis of pleural fluid protein and lactate dehydrogenase alone produces the same categorisation as modified Light's criteria. (bmj.com)
  • Several plasmodial antigens including histidine-rich protein 2 (pHRP-2), plasmodial aldolase, and plasmodial lactate dehydrogenase (pLDH) have been used in RDTs. (biomedcentral.com)
  • The preparation contained less than 0.2% of lactate dehydrogenase isoenzyme-4, was homogeneous by agarose gel electrophoresis and also by polyacrylamide gel electrophoresis at pH 8.9 and 6.9, and showed one major protein band (containing all the enzyme activity) and one minor anodic contaminant (containing no enzyme activity) by analytical isoelectric focusing. (aaccjnls.org)
  • Human lactate dehydrogenase M 4 (the isoenzyme found in skeletal muscle ). (wikipedia.org)
  • Since many enzymes are useful in diagnosing liver diseases, the alteration of the lactate dehydrogenase (LDH) isoenzyme pattern was studied in experimentally induced liver fibrosis. (go.jp)
  • Increase in Lactate Dehydrogenase Isoenzyme-4 and Splenocyte Toxicity in Methomyl-Treated Rats', Arhiv za higijenu rada i toksikologiju , 49(3), str. (srce.hr)
  • 4. Some conclusions about the reactions catalysed by the M 4 isoenzyme were drawn from a comparison of these results with those obtained with the H 4 isoenzyme and liver alcohol dehydrogenase. (biochemj.org)
  • Lactate dehydrogenase 5 (LDH5) is a major lactate dehydrogenase isoenzyme catalyzing the transformation of pyruvate to lactate to provide anaerobic energy. (karger.com)
  • The lactate dehydrogenase (LDH) isoenzyme test checks how much of the different types of LDH are in the blood. (adam.com)
  • Purification of lactate dehydrogenase isoenzyme-5 from human liver. (aaccjnls.org)
  • Lactate dehydrogenase (also called lactic acid dehydrogenase, or LDH) is an enzyme found in almost all body tissues. (kidshealth.org)
  • Lactate dehydrogenase (LDH) is an oxidoreductase enzyme that catalyses the interconversion of pyruvate and lactate. (sigmaaldrich.com)
  • lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. (prospecbio.com)
  • A sequence analysis of the enzyme reveals that it contains an Fe-S oxidoreductase domain in addition to a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain, which differs from other typical d -iLDHs. (asm.org)
  • Distribution of lactate dehydrogenase (and its E-isozymes) in the developing and adult retina of the guppy (Lebistes reticulatus) . (springer.com)
  • Specialized lactate dehydrogenase isozymes: The molecular and genetic basis for the unique eye and liver LDHs of teleost fishes. (springer.com)
  • Developmental genetics of the lactate dehydrogenase isozymes of fish. (springer.com)
  • The inheritance of tissue-specific lactate dehydrogenase isozymes in interspecific bass (Mievoptevus) hybrids. (springer.com)
  • Developmental and biochemical genetics of lactate dehydrogenase isozymes in fishes, p. 243-276. (springer.com)
  • Evolution of the lactate dehydrogenase isozymes of fishes. (springer.com)
  • Its electrophoretic mobility, heat stability, kinetic behavior with pyridine nucleotide analogs, and chromatographic characteristics on diethylaminoethyl cellulose were intermediate to those observed for lactate dehydrogenase isozymes 3 and 4. (sciencemag.org)
  • Rabbit lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. (innov-research.com)
  • This gene encodes the B subunit of lactate dehydrogenase enzyme, which catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+ in a post-glycolysis process. (wikipedia.org)
  • My test means is useful for the qualitative detection and quantitative determination of lactate dehydrogenase in sera wherein the test means comprises a reagent composition incorporated within a bibulous carrier. (freepatentsonline.com)
  • The quantitative determination of lactate dehydrogenase is extremely important in the detection of heart diseases, especially heart attacks, in that, following heart attacks, the concentration of lactate dehydrogenase in the blood rises noticeably over its normal concentration. (freepatentsonline.com)
  • For quantitative determination of lactate dehydrogenase LDH activity and screen/evaluation of LDH modulators. (bioassaysys.com)
  • This subpathway is part of the pathway pyruvate fermentation to lactate, which is itself part of Fermentation. (uniprot.org)
  • View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-lactate from pyruvate , the pathway pyruvate fermentation to lactate and in Fermentation . (uniprot.org)
  • Lactate Dehydrogenase Activity Assay Kit has been used for measuring the activity of lactate dehydrogenase (LDH) in the cell culture medium. (sigmaaldrich.com)
  • Lactate Dehydrogenase Activity Assay Kit has been used to determine the concentration of lactate dehydrogenase in samples. (sigmaaldrich.com)
  • Candidate enzymes include aspartate aminotransferase, alanine aminotransferase, lactate dehydrogenase (LD), and alkaline phosphatase [ 6 ]. (hindawi.com)
  • This study evaluated the prognostic value of alkaline phosphatase (ALP) and lactate dehydrogenase (LDH) together with host-related factors in patients with unresectable advanced gastric cancer. (springermedizin.de)
  • The enzyme is also found in cerebrospinal fluid where high levels of lactate dehydrogenase in cerebrospinal fluid are often associated with bacterial meningitis . (bionity.com)
  • A diagnostic test indicator for the determination of the concentration of lactate dehydrogenase in sera comprising a bibulous material which has contained therein the dried residue resulting from the impregnation thereof with 1. (freepatentsonline.com)
  • 1. A diagnostic test indicator for the determination of the concentration of lactate dehydrogenase in sera comprising a bibulous material which contains therein the dried residue resulting from the impregnation thereof with 2. (freepatentsonline.com)
  • Available tests for the detection of the concentration of lactate dehydrogenase in body fluids have, until now, consisted of extremely complex liquid systems whereby test tubes, measuring devices, ultraviolet light, standardization of instruments, correction factors depending upon temperature and false readings prevail. (freepatentsonline.com)
  • As mentioned briefly above, I have now discovered a novel test means for the determination of the concentration of lactate dehydrogenase in body fluids. (freepatentsonline.com)
  • Mutations in this gene are associated with lactate dehydrogenase B deficiency. (wikipedia.org)
  • Entrez Gene: Lactate dehydrogenase B". Retrieved 2017-10-01. (wikipedia.org)
  • One of the most interesting gene products investigated is the enzyme lactate dehydrogenase (LDH), particularly the isozyme of LDH found in the retina of many groups of teleosts (Markert and Faulhaber, 1965). (springer.com)
  • Lactate dehydrogenase ontogeny, paternal gene activation, and tetramer assembly in embryos of brook trout, lake trout, and their hybrids. (springer.com)
  • Homology of lactate dehydrogenase genes: E gene function in the teleost nervous system. (springer.com)
  • We showed that LDHD expression is enriched in tissues with a high metabolic rate and abundant mitochondria and that d-lactate dehydrogenase resides in the mitochondria of cells overexpressing the human LDHD gene. (jci.org)
  • Identification of a novel human lactate dehydrogenase gene LDHAL6A, which activates transcriptional activities of AP1(PMA). (sigmaaldrich.com)
  • An example is the gene that encodes an enzyme called lactate dehydrogenase (LDH). (elifesciences.org)
  • The gene encoding l-lactate dehydrogenase from Thermoanaerobacterium saccharolyticum JW/SL-YS485 was cloned, sequenced, and used to obtain an l-ldh deletion mutant strain (TD1) following a site-specific double-crossover event as confirmed by PCR and Southern blot. (semanticscholar.org)
  • The bifunctional alcohol and aldehyde dehydrogenase gene, adhE, is necessary for ethanol production in Clostridium thermocellum and Thermoanaerobacterium saccharolyticum. (semanticscholar.org)
  • In cardiac muscle, lactate dehydrogenase converts lactate to pyruvate, which can participate in other chemical reactions to create energy. (medlineplus.gov)
  • Lee Biosolutions produces Porcine Muscle Lactate Dehydrogenase (LDH) for medical research, life science and diagnostic manufacturing uses. (leebio.com)
  • 5. With human and rat liver homogenates and with purified human liver glycollate oxidase and rabbit muscle lactate dehydrogenase, dl -phenyl-lactate (2 mmol/l) completely inhibits glycollate oxidase but has no effect on lactate dehydrogenase. (portlandpress.com)
  • The aim of this study was to determine the usefulness of a new kit that can evaluate salivary lactate dehydrogenase (LD) level in real time for screening gingivitis. (hindawi.com)
  • This study aims to determine the best storage condition for salivary lactate dehydrogenase due to decreased in native enzyme s activity after seven days of storage. (scialert.net)
  • On the other hand, glycerol managed to stabilize salivary lactate dehydrogenase activity for two weeks at 4 and -20°C. As conclusion, polyethylene glycol showed as the best additive for salivary lactate dehydrogenase storage whereas, ethylenediaminetetraacetic acid suitable only at room temperature for a week. (scialert.net)
  • Human LDH Isoenzymes, also known as lactic dehydrogenase, are responsible for converting muscle lactic acid into pyruvic acid, an essential step in producing cellular energy. (webwire.com)
  • The enzyme lactate dehydrogenase (also known as lactic dehydrogenase, or LDH) is found in the cells of almost all body tissues. (thefreedictionary.com)
  • a nicotinamide-adenine-dinucleotide- an alkali Lactate salt mixture and a process for the production of said indicator, are disclosed. (freepatentsonline.com)
  • This test measures the amount of the enzyme lactate dehydrogenase (LDH) in your cerebrospinal fluid (CSF). (ahealthyme.com)
  • Lactate dehydrogenase and aspartete transaminase of the cerebrospinal fluid in patients with brain tumours, congenital hydrocephalus, and brain abscess. (bmj.com)
  • In some people with lactate dehydrogenase-A deficiency, high-intensity exercise or other strenuous activity leads to the breakdown of muscle tissue (rhabdomyolysis). (medlineplus.gov)
  • Affected individuals are usually discovered only when routine blood tests reveal reduced lactate dehydrogenase activity. (medlineplus.gov)
  • When muscle cells do not get sufficient energy during exercise or strenuous activity, the muscles become weak and muscle tissue can break down, as experienced by people with lactate dehydrogenase-A deficiency. (medlineplus.gov)
  • Even though lactate dehydrogenase activity is decreased in the cardiac muscle of people with lactate dehydrogenase-B deficiency, they do not appear to have any signs or symptoms related to their condition. (medlineplus.gov)
  • Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. (ebi.ac.uk)
  • Localization of lactate dehydrogenase activity in the cells of the fish (Xiphophorus hellevi) eye. (springer.com)
  • Measurement of released lactate dehydrogenase (LDH) activity, a commonly used marker of lethal cell injury in both in vitro and in vivo screenings, has been used to assess the cytotoxicity of nanoparticles (NPs), chemical compounds, and environmental factors. (nih.gov)
  • Lactate dehydrogenase ( LDH ) activity in the supernatant and TiO 2 nanoparticle ( NP ) re-suspension. (nih.gov)
  • LDH activity can be easily quantified by using the NADH produced during the conversion of lactate to pyruvate to reduce a second compound in a coupled reaction into a product with properties that are easily quantitated. (chemie.de)
  • In experiments described here high levels of a lactate dehydrogenase k activity were detected in extracts of normal rodent retina. (sciencemag.org)
  • Here, we demonstrate the self-organization of L-lactate dehydrogenase (LDH), which exhibits enhanced enzymatic activity and stability on a variety of gold surfaces ranging from nanoparticles to electrodes, by incorporating a gold-binding peptide tag (AuBP2) as the fusion partner for Bacillus stearothermophilus LDH (bsLDH). (nih.gov)
  • Lactate dehydrogenase activity in blood lymphocytes changed similarly in aggressive and submissive mice probably due to social stress. (springer.com)
  • The activity of succinate dehydrogenase changed differently and correlated with the type of social behavior. (springer.com)
  • The FAD-containing dehydrogenase domain retained 2-hydroxyacid-oxidizing activity, although it decreased compared to the full Fe-S d -iLDH. (asm.org)
  • Plasma lactate dehydrogenase: a marker of disease activity in cryptogenic fibrosing alveolitis and extrinsic allergic alveolitis? (ersjournals.com)
  • Total plasma lactate dehydrogenase (LDH) activity may be elevated in cryptogenic fibrosing alveolitis (CFA) and extrinsic allergic alveolitis (EAA), and may be a useful monitor of disease progress. (ersjournals.com)
  • 4. Is this assay for lactate dehydrogenase activity affected by which anticoagulant is used in the blood draw? (bioassaysys.com)
  • Can Lactate Dehydrogenase be used to Index Anaerobic Activity in Fishe" by Casey W. Schoenebeck, Erik Prenosil et al. (unl.edu)
  • Can Lactate Dehydrogenase be used to Index Anaerobic Activity in Fishes? (unl.edu)
  • This study experimentally evaluated if the muscle enzyme lactate dehydrogenase (LDH) can be used to index recent anaerobic activity in fish by testing the hypothesis that muscle LDH activity will be greater in exercised fish than in rested fish. (unl.edu)
  • This assay is a fast and simple method to determine changes in the plasma membrane upon incubation with a test compound LDH activity reduces pyruvate to lactate by oxidizing NADH to NAD+. (aniara.com)
  • This unique functional interaction between LDH family members supports lactate dehydrogenase activity in the sperm. (researchmap.jp)
  • 0.01) at all three temperatures compared to Lactate dehydrogenase basal activity. (scialert.net)
  • The aim of the present work was to analyze changes in lactate dehydrogenase (LDH) activity in the cytoplasm of neurons in the hippocampus and cerebral cortex on Mongolian gerbils ( Meriones unguiculatus ) in the early and late reperfusion periods after global ischemia. (springer.com)
  • LDH catalyzes the conversion of lactate to pyruvic acid and back, as it converts NAD + to NADH and back. (wikipedia.org)
  • Lactate dehydrogenase catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD + . (wikipedia.org)
  • S)-lactate + NAD + = pyruvate + NADH. (uniprot.org)
  • 1. The very fast pre-steady-state formation of NADH catalysed by pig M 4 lactate dehydrogenase was equivalent to the enzyme-site concentration at pH values greater than 8.0 and to one-half the site concentration at pH6.8. (biochemj.org)
  • 2. The rate of dissociation of NADH from the enzyme at pH8.0 (450s −1 ) in the absence of other substrates is faster than the steady-state oxidation of lactate (80s −1 ). (biochemj.org)
  • One unit will catalyze the oxidation of one micromole of L-lactate to pyruvate with simultaneous reduction of NAD+ to NADH per minute at 37°C and pH 9.4. (leebio.com)
  • The Warburg effect is the enhanced conversion of glucose to lactate observed in tumor cells, even in the presence of normal levels of oxygen. (sigmaaldrich.com)
  • At high concentrations of lactate, the enzyme exhibits feedback inhibition, and the rate of conversion of pyruvate to lactate is decreased. (wikipedia.org)
  • If the conversion of pyruvate to lactate is reduced, cells excessively use the oxidative phosphorylation flux as a metabolic pathway to generate ATP, resulting in ROS due to oxidative stress, eventually leading to cell death 14 . (nature.com)
  • A tetrameric enzyme that, along with the coenzyme NAD+, catalyzes the interconversion of LACTATE and PYRUVATE. (harvard.edu)
  • Lactate dehydrogenase deficiency is a condition that affects how the body breaks down sugar to use as energy in cells, primarily muscle cells. (medlineplus.gov)
  • There are two types of this condition: lactate dehydrogenase-A deficiency (sometimes called glycogen storage disease XI) and lactate dehydrogenase-B deficiency. (medlineplus.gov)
  • People with lactate dehydrogenase-A deficiency experience fatigue, muscle pain, and cramps during exercise (exercise intolerance). (medlineplus.gov)
  • Some people with lactate dehydrogenase-A deficiency develop skin rashes. (medlineplus.gov)
  • The severity of the signs and symptoms among individuals with lactate dehydrogenase-A deficiency varies greatly. (medlineplus.gov)
  • People with lactate dehydrogenase-B deficiency typically do not have any signs or symptoms of the condition. (medlineplus.gov)
  • Lactate dehydrogenase deficiency is a rare disorder. (medlineplus.gov)
  • the prevalence of lactate dehydrogenase deficiency in other countries is unknown. (medlineplus.gov)
  • Lactate dehydrogenase deficiency can probably be considered a non-disease. (abcam.com)
  • Lactate dehydrogenase deficiency type C: A rare genetic disorder where an enzyme deficiency (Lactate dehydrogenase type C) affects the conversion of carbohydrates to energy. (checkorphan.org)
  • The list of signs and symptoms mentioned in various sources for Lactate dehydrogenase deficiency type C includes the 1 symptoms listed below: * Asymptomatic Note that Lactate dehydrogenase deficiency type C symptoms usually refers to various symptoms known to a patient, but the phrase Lactate dehydrogenase deficiency type C signs may refer to those signs only noticable by a doctor. (checkorphan.org)
  • The signs and symptom information on this page attempts to provide a list of some possible signs and symptoms of Lactate dehydrogenase deficiency type C. This medical information about signs and symptoms for Lactate dehydrogenase deficiency type C has been gathered from various sources, may not be fully accurate, and may not be the full list of Lactate dehydrogenase deficiency type C signs or Lactate dehydrogenase deficiency type C symptoms. (checkorphan.org)
  • Furthermore, signs and symptoms of Lactate dehydrogenase deficiency type C may vary on an individual basis for each patient. (checkorphan.org)
  • Only your doctor can provide adequate diagnosis of any signs or symptoms and whether they are indeed Lactate dehydrogenase deficiency type C symptoms. (checkorphan.org)
  • The diagnostic value of CSF lactate dehydrogenase and aspartate transaminase in cases of brain tumours (except for CSF AST in the benign tumours), congenital hydrocephalus, and brain abscess is established. (bmj.com)
  • On the other hand, LDH also serves to remove lactate during aerobic recovery, especially in tissues such as liver or heart. (biologists.org)
  • Lactate dehydrogenase (LDH) catalyses the last step of aerobic glycolysis, the pyruvate to lactate conversion. (bmj.com)
  • D-lactate dehydrogenase (cytochrome) ) and L-lactate ( L-lactate dehydrogenase (cytochrome) ). (wikipedia.org)
  • Compared to the intact enzyme, the FAD-containing dehydrogenase domain showed increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely lost the ability to use coenzyme Q 10 . (asm.org)
  • Malate dehydrogenases that catalyse the interconversion of malate to oxaloacetate and participate in the citric acid cycle, and L-2-hydroxyisocaproate dehydrogenases are also members of the family. (wikipedia.org)
  • Malate dehydrogenases catalyse the interconversion of malate to oxaloacetate [ PMID: 8117664 ]. (ebi.ac.uk)
  • The book entitled "Lactate Dehydrogenase (LDH): Biochemistry, Functions and Clinical Significance" provides a broad and authoritative review of the lactate dehydrogenase enzyme, including its isoforms, catalytic functions, distribution in various tissues, involvement in cancer cell metabolism and tumorigenesis, involvement in the plasmodium enzyme, various small molecule inhibitors of hLDHA and pfLDH, and clinical significance. (novapublishers.com)
  • These genes provide instructions for making the lactate dehydrogenase-A and lactate dehydrogenase-B pieces (subunits) of the lactate dehydrogenase enzyme. (medlineplus.gov)
  • Evidence for historical, demographic and selective factors affecting enzyme evolution can be obtained by examining nucleotide sequence variation in candidate genes such as Lactate dehydrogenase ( Ldh ). (biomedcentral.com)
  • Many cancer cells produce ATP through high-level lactic acid fermentation catalyzed by lactate dehydrogenase (LDH), which converts pyruvic acid to lactic acid. (nature.com)
  • Immunohistochemistry-Paraffin: Lactate Dehydrogenase C Antibody [NBP1-92065] - Staining in human testis and prostate tissues using anti-LDHC antibody. (novusbio.com)
  • Immunohistochemistry-Paraffin: Lactate Dehydrogenase C Antibody [NBP1-92065] - Staining of human testis shows strong cytoplasmic and nuclear positivity in cells in seminiferus ducts. (novusbio.com)
  • Immunohistochemistry-Paraffin: Lactate Dehydrogenase C Antibody [NBP1-92065] - Staining of human prostate shows low expression as expected. (novusbio.com)
  • Plasmodium lactate dehydrogenase (pLDH) is a major target in diagnosing the erythrocytic stage of malaria parasites because it is highly expressed during blood-stage parasites and is distinguished from human LDH. (biomedcentral.com)
  • L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis [ PMID: 11276087 ]. (ebi.ac.uk)
  • Malate and lactate dehydrogenases (MDH and LDH) are homologous, core metabolic enzymes that share a fold and catalytic mechanism yet possess strict specificity for their substrates. (elifesciences.org)
  • The enzyme had a mean pI value of 9.59 (SD 0.04) (n = 5) at 5 degrees C. By comparison, the pI value of a preparation of rabbit lactate dehydrogenase-5 was 9.16 (5 degrees C). (aaccjnls.org)
  • Association of the testicular lactate dehydrogenase isozyme with a special type of mitochondria. (springer.com)
  • Lactate dehydrogenase isozyme patterns of fish. (springer.com)
  • Lactate dehydrogenase isozyme synthesis and cellular differentiation in the teleost retina. (springer.com)
  • An unusual isozyme of lactate dehydrogenase, lactate dehydrogenase k, is found in high concentrations in cultured cells transformed by the Kirsten murine sarcoma virus and in many human cancer tissues. (sciencemag.org)
  • A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. (wikipedia.org)
  • During the final stage of glycogen breakdown, lactate dehydrogenase converts a molecule called pyruvate to a similar molecule called lactate. (medlineplus.gov)
  • Lactate dehydrogenase (LDH) is a hydrogen transfer enzyme that catalyzes the oxidation of l -lactate to pyruvate with the mediation of NAD + as a hydrogen acceptor, with the reaction being reversible. (degruyter.com)
  • Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD). (prospecbio.com)
  • Such an oxidation occurs during the reversible transformation of pyruvate to lactate, a reaction catalyzed by lactate dehydrogenase (LDH) 5 [ 7 ]. (karger.com)
  • Lactate dehydrogenase is composed of four subunits (tetramer). (wikipedia.org)
  • Various combinations of the lactate dehydrogenase-A and lactate dehydrogenase-B subunits make up the different forms of the enzyme. (medlineplus.gov)
  • The version of lactate dehydrogenase made of four lactate dehydrogenase-B subunits is found primarily in heart (cardiac) muscle . (medlineplus.gov)
  • It converts pyruvate, the final product of glycolysis , to lactate when oxygen is absent or in short supply, and it performs the reverse reaction during the Cori cycle in the liver . (wikipedia.org)
  • We clarified that lactate dehydrogenase C (LDHC), a testis-specific lactate dehydrogenase, is responsible for L-2-HG accumulation by generating and analysing Ldhc-deficient mice. (researchmap.jp)
  • Binding of titanium dioxide nanoparticles to lactate dehydrogenase. (nih.gov)
  • Lactate Dehydrogenase B Polyclonal antibody specifically detects Lactate Dehydrogenase B in Human, Mouse, Rat samples. (fishersci.com)