Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LACTATE DEHYDROGENASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 667 records · Page 37Linked to original sources
PubMed1996

Electrophoretic study of lactate dehydrogenase and alkaline phosphatase isoenzymes of the Mongolian gerbil (Meriones unguiculatus).

Lactate dehydrogenase and alkaline phosphatase isoenzymes of the Mongolian gerbil were examined using electrophoretic techniques and were compared with those of the mouse, rat, and guinea pig. Five isoenzymes of lactate dehydrogenase (LDH) were detected in the gerbil with LDH2 and LDH5 being equally dominant. Two bands of alkaline phosphatase (ALP) were distinguished in sera treated with neuraminidase in the gerbil and the relative activity of the cathodic fraction was greater than those of the mouse and rat. Genetic polymorphism was not found among the coat color variants of the Mongolian gerbil. A comparative study on LDH and ALP revealed distinct interspecific differences in the rate of the electrophoretic migration of the respective isoenzymes among the mouse, rat, guinea pig, and the Mongolian gerbil.

Alkaline Phosphatase↗
PubMed1975

[Activity of lactate dehydrogenase in the dairy cow milk serum in relation to positive mastitis test NK].

The level of total lactate dehydrogenase activity in dairy cow milk serum was studied in sets of quarter-udder milks showing different degrees of a positive response to Mastitis test-NK. The bacteriological examination for Streptococcus agalactiae, Streptococcus dysgalactiae, Streptococcus uberis, Staphylococcus aureus, and for coliform germs was performed at the same time. Increasing positiveness of the response to Mastitis test-NK was found to be accompanied by almost proportionate increase of the total lactate dehydrogenase activity level in milk serum. The bacteriological finding was not correlated with increasing positiveness of the response to Mastitis test-NK. New aspects of various diseases of the mammary gland and the possibility to diagnose mainly the latent stages of these diseases are analysed in a discussion. milk serum, optical test; lactate dehydrogenase level; bacteriological finding.

Animals↗
PubMed1991

Lactate dehydrogenase activity as a cause of metronidazole resistance in Bacteroides fragilis NCTC 11295.

Enzymes acting on pyruvate as a parameter of the ATP regeneration system were studied as a cause of metronidazole resistance in Bacteroides fragilis NCTC 11295. The resistant strain had higher lactate dehydrogenase activity and produced more lactate than susceptible strains, suggesting that the enzyme is more active in lactic acid fermentation. Furthermore, the reaction catalysed by lactate dehydrogenase occurred up to 48 mg/L metronidazole, whereas the reaction catalysed by pyruvate: ferredoxin oxidoreductase reaction stopped at 2 mg/L. The mechanism of metronidazole resistance in B. fragilis NCTC 11295 may be due to the high activity of lactate dehydrogenase which compensates for the decreased activity of pyruvate: ferredoxin oxidoreductase in the presence of metronidazole.

Adenosine Triphosphate↗
PubMed1980

Hereditary deficiency of lactate dehydrogenase M-subunit.

A family with a complete deficiency of lactate dehydrogenase M-subunit was investigated. The propositus was an 18-year-old male who complained of exertional pigmenturia and easy fatigue. Marked discrepancy was observed in the ratio between creatine kinase and lactate dehydrogenase (CK/LDH). Electrophoretic analysis of serum LDH isoenzymes of the propositus demonstrated only one activity band of LDH H4. A complete lack of the LDH M-subunit was similarly demonstrated in erythrocytes, leukocytes and in the intermediate vastus muscle. LDH levels in the muscle specimen were markedly decreased in the patient, whereas CK and aspartate aminotransferase were almost the same as in a control subject. LDH isoenzymes of erythrocytes were analyzed in 5 siblings and in the parents. This demonstrated a complete lack of LDH M-subunit in 3 siblings. The ratio between H-subunit and M-subunit (H/M) in erythrocyte LDH suggested a partial absence of the M-subunit in two siblings and in the parents. An abortive increase of blood lactate and a marked increase in blood pyruvate were observed immediately after ischemic work of the forearm, accompanied by an increase in serum creatine kinase and myoglobinuria. The present case represents a newly described form of genetically determined myopathy.

Adolescent↗
PubMed1991

The lactate dehydrogenase of the icefish heart: biochemical adaptations to hypoxia tolerance.

Cardiac lactate dehydrogenase from the hemoglobin- and myoglobin-free antarctic icefish has been purified by affinity chromatography. Structural and kinetic properties of the enzyme were found close or identical to those of its skeletal muscle counterpart and other M-type lactate dehydrogenases. A model involving a dual oxidative-anaerobic metabolism of the icefish heart is proposed.

Acclimatization↗
PubMedDate not supplied

Serum lactate dehydrogenase isoenzymes in the diagnosis of myocardial infarction.

The ratio of lactate dehydrogenase (LD-1:LD-2) in serum was studied in 101 patients admitted to a coronary care unit. The clinical reliability of the test could not be predicted from the normality or abnormality of the total serum lactate dehydrogenase (LD) activity. However, for samples with total LD activity below the middle of the normal range, no information was provided by the test. In contrast, the test provided reliable information when the total LD activity in the specimen was above the middle of the reference range (220 IU per L).

Electrophoresis↗
PubMed1976

Thermodynamic studies of binary and ternary complexes of pig heart lactate dehydrogenase.

The thermodynamics of the reaction catalyzed by pig heart muscle lactate dehydrogenase (LDH; EC1.1.1,27) have been studied in 0,2 M potassium phosphate buffer, pH 7, over the temperature range of 10 to 35 degrees C by using oxamate and oxalate to simulate the corresponding reactions of the substrates pyruvate and lactate, respectively. The various complexes formed are characterized by Gibbs free energies, enthalpies, and entropies. The Gibbs free energies were determined by equilibrium dialysis investigations, fluorescence titrations, and ultraviolet difference spectroscopy, while the reaction enthalpies stem from direct calorimetric measurements, Formulas are given for both the temperature dependence of the equilibrium constants and the variation with temperature of the enthalpies involved in the four reactions between LDH and NADH or NAD, LDH-NADH and oxamate, and LDH-NAD and oxalate. All reactions show a marked negative temperature coefficient, deltacp, of the binding enthalpies indicating partial refolding to be associated with binary and ternary complex formation. This interpretation appears very probable in view of recent x-ray crystallographic studies on lactate dehydrogenase from dogfish, which demonstrate a volume decrease to occur on binding of oxamate to the LDH-NADH complex. The validity of the thermodynamic parameters, as derived with substrate analogues, for the actual catalytic reaction, gains strong support from the agreement between the sum of the heats involved in the four intermediary reactions reported in this study and direct determinations of the overall enthalpy associated with the catalytic process published in the literature.

Animals↗
PubMed1998

Amperometric immunosensor for lactate dehydrogenase LD-1.

An amperometric immunosensor for the detection of the lactate dehydrogenase isoenzyme LD-1 has been developed. Polyclonal antibodies for LD-1 have been covalently immobilised onto a preactivated Immunodyne ABC membrane, reacted with standard LD-1 solutions and placed onto a platinum working electrode polarised at +600 mV vs. Ag/AgCl. Lactate dehydrogenase activity has been measured by detection of the oxidation of NADH at the electrode surface. A calibration curve for LDH in the 0.005-0.12 U range has been obtained with a repeatability of 3% and a reproducibility of 10%. The probe exhibited good selectivity (response of LD-2 was 18% of LD-1) which was further improved using thermal treatment of the membranes. Measurement of LD-1 content in human control serum with the developed procedure gave a LD-1 concentration in the reported assigned range.

Animals↗
PubMed1968

Lactate dehydrogenase isozymes in parthenogenetic teiid lizards (Cnemidophorus).

Heterozygosity occurs at the lactate dehydrogenase b-locus in two diploid parthenogenetic species of Cnemidophorus. Each such species produces two different B subunits, one of which is also found in two sexual species and in two triploid parthenogenetic species; the other occurs also in a third sexual species. Interspecific hybridization between sexual species carrying different b-alleles and producing different B subunits may be responsible for the heterozygosity at the lactate dehydrogenase b-locus in diploid parthenogenetic Cnemidophours.

Animals↗
PubMed1978

Isolation of human lactate dehydrogenase isoenzyme X by affinity chromatography.

Human isoenzyme LDH-X (lactate dehydrogenase isoenzyme X) was isolated from seminal fluid of frozen semen samples by affinity chromatography by using oxamate-Sepharose and AMP-Sepharose. In the presence of 1.6 mM-NAD+, isoenzyme LDH-X does not bind to AMP-Sepharose, whereas the other lactate dehydrogenase isoenzymes do. This is the crucial point in the isolation of isoenzyme LDH-X from the other isoenzymes. The purified human isoenzyme LDH-X had a specific activity of 146 units/mg of protein.

Adenosine Monophosphate↗
PubMedDate not supplied

[Influence of loach egg- and embryo-extract on the activity of lactate dehydrogenase in the presence of insulin].

Studies of the pig muscle lactate dehydrogenase (LDH) activity were permormed after incubating the enzyme solution with extracts of loach (Misgurnus fossilis) eggs and embryos, which were subjected to the influence of insulin hydrocortisone as well as to insulin combination with actinomycin D, cycloheximide or puromycin. The insulin alone is established to decrease the inactivating ability of the investigated extracts on the lactate dehydrogenase activity, when antibiotics removed to a considerable extent the influence of hormone. In the eggs and embryos there are proteins activating and stabilizing the LDH molecule. The level of LDH activation under the influence of the eggs and embryos extracts subjected to the insulin action was decreased. The addition of hydrocortisone to the medium for the incubation of eggs and embryos does not affect significantly the LDH-inactivating ability of their extracts.

Animals↗
PubMedDate not supplied

[Regularities in the kinetic of photoactivation of lactate dehydrogenase by the action of UV light in different microenvironment].

The kinetics of photoinactivation of cardiac (H4) and muscular (M4) isoforms of lactate dehydrogenase irradiated by UV light (240-390 nm) in the free form and in the presence of sodium azide, D-mannitol, and serotonin was studied. It was shown that the decrease in the catalytic activity of both enzymes can be described by the kinetics of the first-order monomolecular reaction. The inactivation rate constant of lactate dehydrogenase M4 is considerably higher than that of lactate dehydrogenase H4, indicating a greater photochemical lability of the isoform M4. It was shown that sodium azide has a different protective action on the proteins studied. The irradiation of the muscular isoform in the presence of serotonin and D-mannitol did not change the character of the "dose-effect" curve and only led to a decrease in the photoinactivation rate constant of the protein.

Animals↗
PubMed1995

Nature and environment of the sulfhydryls of membrane-associated D-lactate dehydrogenase of Escherichia coli.

Ellman's reagent, 5,5'-dithiobis(2-nitrobenzoic acid), has been used to titrate D-lactate dehydrogenase (D-LDH), a respiratory flavoenzyme of Escherichia coli. All six of the possible sulfhydryls titrate in the presence of 2% sodium dodecylsulfate, showing that D-lactate dehydrogenase does not contain any -S-S- bridges. In the native state, only two sulfhydryls are accessible in buffer and only one in the presence of lipid. Single-site mutations of each of the six cysteines of D-lactate dehydrogenase have been prepared. Each of the purified mutant proteins has full activity, demonstrating that an -SH group is not essential to the FAD-driven redox reaction. Ellman's titrations of the mutant proteins have led to the identification of cysteines 65, 146, 156, and 256 in the amino-terminal end as those containing the sulfhydryls that are not accessible in buffer or in buffer plus lipid. The cysteine at 422 is titrated only partially in buffer, while in buffer containing lipid, a necessary factor for full enzymatic activity, its sulfhydryl is inaccessible to the reagent. Cysteine 492 has been identified as containing the sulfhydryl that is accessible to the reagent under both conditions.

Bacterial Outer Membrane Proteins↗
PubMed1978

[Serum lactate dehydrogenase isoenzyme spectrum in malignant neoplasm patients].

The isoenzymic spectrum of lactate dehydrogenase of blood sera was studied in 170 patients with malignant and benign tumors, chronic inflammatory lesions and in healthy persons. The characteristic changes in patients with malignant tumors were as follows: an increased activity of slow fractions and a decreased one in rapidly migrating fractions. The level of the 5th isoenzyme activity and the frequency of its increased activity in serum correlated well with the degree of cancer spread. The determination of a percentual content of the isoenzyme may be used as a supplementary test for diagnosing metastic involvement of the liver. The examination of the serum lactate dehydrogenase spectrum in patients with benign tumors and chronic inflammatory disease revealed no changes characteristic of malignant neoplasms.

Female↗
PubMed1990

Cloning and expression of the gene encoding the fructose-1,6-diphosphate-dependent L-(+)-lactate dehydrogenase of Streptococcus mutans.

The fructose-1,6-diphosphate-dependent lactate dehydrogenase from Streptococcus mutans JH1000 was purified by a modification of published methods. The sequence of 27 amino-terminal amino acids was determined, which allowed us to construct a 17-base DNA probe that had 32-fold degeneracy. The probe was used to screen a genomic library in pBR322. Of 18 reactive clones, 1 was found that expressed lactate dehydrogenase (LDH) activity identical to that of S. mutans with regard to dependence on fructose-1,6-diphosphate, thermal inactivation profile, and inhibition by sodium oxamate. Extracts of this clone possessed a protein band that comigrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with purified LDH from JH1000. Compared with controls, the clone was shown to produce elevated amounts of L-(+)-lactic acid during growth in the presence of glucose, thereby indicating that the activity was expressed in vivo. This result was substantiated by demonstrating that the activity could complement a mutation in the fermentative D-(-)-LDH of Escherichia coli. Subcloning showed that the S. mutans LDH subunit is encoded by a 1.2-kilobase gene. Our ability to clone this gene is expected to have great practical significance in the construction of an effector strain for use in the replacement therapy of dental caries.

Amino Acid Sequence↗
PubMed1981

LDHk, an unusual oxygen-sensitive lactate dehydrogenase expressed in human cancer.

An unusual isozyme of lactate dehydrogenase (LDH; L-lactate:NAD+ oxidoreductase, EC 1.1.1.27), LDHk, has been described in cells transformed by the Kirsten murine sarcoma virus (KiMSV). This isozyme appears to contain one or more subunits encoded by the transforming gene of KiMSV and is readily distinguished from other isozymes of LDH. Specifically, it is more basic than other LDH isozymes, has an apparent subunit structure of (35,000)4(22,000)1, is essentially inactive if assayed under a normal atmosphere, and is strongly inhibited by GTP and various related compounds. We have examined human cancer and normal tissue controls for expression of an activity like LDHk. In 11 out of 16 human carcinomas, LDHk activity was increased 10- to 500-fold over the level seen in adjoining nontumor tissue. In contrast, other LDH isozymes were increased by only 2- to 5-fold.

Aerobiosis↗
PubMed2003

Inhibition of lactate dehydrogenase C4 (LDH-C4) blocks capacitation of mouse sperm in vitro.

Lactate dehydrogenase C4 (LDH-C4) is a tissue-specific enzyme in the mammalian testis and the only lactate dehydrogenase isozyme of sperm. Inhibitors of LDH activity were used to determine whether this enzyme plays a role in sperm capacitation, the acrosome reaction and/or fertilization. Oxamate or its derivative was used to inhibit sperm LDH activity in a medium promoting capacitation. Complete inhibition of LDH activity blocked capacitation. This effect could be reversed partially by the addition of dbcAMP or pentoxifylline to the culture medium. Western blotting showed that oxamate and N-isopropyl oxamate inhibited the tyrosine phosphorylation of proteins during the sperm capacitation process. Presumably, glycolysis is the primary energy pathway for sperm metabolism. The oxidation of reduced NAD with the conversion of pyruvate to lactate by LDH provides ATP necessary for protein kinase A (PKA) activity. Our data indicate that LDH-C4 plays an important metabolic role in sperm capacitation.

Animals↗
PubMed1977

The topography of porcine lactate dehydrogenase isoenzyme H4. The identification of lysines on the surface.

Porcine lactate dehydrogenase isoenzyme H4 was treated with methyl 6-(2,4-dinitrophenylamino)hexanimidate hydrochloride and the lysines modified hereby were identified. For this purpose 20 chymotryptic-tryptic N epsilon-[6-(2,4-dinitrophenylamino)hexanimidoyl]lysine containing peptides were isolated by means of gel chromatography, countercurrent distribution, thin-layer chromatography and ion-exchange chromatography. Their amino acid composition, the amino end groups and their electrophoretic mobilities were determined. With these data, the known primary structure of the procine lactate dehydrogenase isoenzyme H4 and the 6-A resolution structure analysis performed by Rossmann et al.[1] we identified the following lysines on the surface of the quarternary structure of the enzyme: no. 4, 6, 60, 77, 82, 121, 157, 179, 226, 230, 241, 306, 308, 316, 327 and 330. No modified lysine peptides were found in the intersubunit binding sites.

Amino Acid Sequence↗