Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.27 (lactate dehydrogenase)
29,211 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The occurrence and levels of activity of various enzymes of carbohydrate catabolism in culture forms (promastigotes) of 4 human species of Leishmania (L. brasiliensis, L. donovani, L. mexicana, and L. tropica) were compared. These organisms possess enzymes of the Embden-Meyerhof pathway but lack lactate dehydrogenase. No evidence could be found for the production of lactic acid by growing cultures and lactic acid could not be detected either in cell-free preparations or after incubation of cell-free extracts with pyruvate and NADH under appropriate conditions. All 4 species possess alpha-glycerophosphate dehydrogenase and alpha-glycerophosphate phosphatase which together could regenerate NAD, thus compensating for the absence of lactate dehydrogenase. The oxidative and nonoxidative reactions of the hexose monophosphate pathway are present in all 4 species. Cell-free extracts have pyruvate dehydrogenase activity which allows the entry of pyruvate into and its subsequent oxidation through the tricarboxylic acid cycle. All enzymes of this cycle, including a thiamine pyrophosphate dependent alpha-ketoglutarate dehydrogenase, are present. Both NAD and NADP-linked malate dehydrogenase activities are present. The isocitrate dehydrogenase is NADP specific. There is an active glutamate dehydrogenase which could compete with alpha-ketoglutarate dehydrogenase for the common substrate (alpha-ketoglutarate). Replenishment of C4 acids is accomplished by heterotrophic CO2 fixation catalyzed by pyruvate carboxylase. All 4 species have high levels of NADH oxidase activity. Several enzymes thus far not found in any species of Leishmania have been demonstrated. These are: phosphoglucose isomerase, triose phosphate isomerase, fructose-1, 6-diphosphatase, 3-phosphoglycerate kinase, enolase, alpha-glycerophosphate dehydrogenase, alpha-glycerophosphate phosphatase, pyruvate dehydrogenase complex, citrate synthase, aconitase, alpha-ketoglutarate dehydrogenase, glutamate dehydrogenase, and NADH oxidase.
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PMID:Enzymes of carbohydrate metabolism in four human species of Leishmania: a comparative survey. 100 46

In extracts of rabbit bone marrow cells was studied effect of erythropoietine on the activity of some enzymes (hexokinase, phosphoglucomutase, phosphohexoisomerase, lactate dehydrogenase, glucoso-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and NADP-reductase). The NADP-reductase activity was increased under the effect of erythropoietine; the activities of other enzymes studied was not altered.
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PMID:[Study of the mechanism of erythropoietin effect on energy metabolism in the bone marrow]. 103 Aug 78

1. The effects of protein concentration and ionic strength on the adsorption of the individual glycolytic enzymes to F-actin and F-actin--trypomyosin--troponin have been studied. 2. Appreciable association was demonstrated under conditions of physiological ionic strength and high protein concentration, and tropomyosin--troponin established as an important and generalized component of these interactions. 3. Phosphofructokinase, aldolase, pyruvate kinase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and glucose-6-phosphate isomerase were strongly bound under these conditions, while triosephosphate isomerase, phosphoglycerate kinase, phosphoglycerate mutase, enolase and hexokinase displayed less adsorption to the structural proteins. 4. The influence of a number of parameters on the adsorption phenomena was examined. Ca2+ and fructose 1,6-diphosphate increased the adsorption of aldolase, lactate dehydrogenase and pyruvate kinase, while decreasing the adsorption of the enzymes of the constant-proportion group. 5. Of the other major enzymic components of skeletal muscle, creatine kinase, adenylate kinase and malate dehydrogenase showed no adsorption to F-actin--tropomyosin--troponin under the experimental conditions. Some adsorption was evident, however, in the case of aspartate aminotransferase, (NADP) isocitrate dehydrogenase and alpha-glycerolphosphate dehydrogenase. 6. These results have been discussed in relation to their functional significance and the roles of enzyme compartmentation in the cell.
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PMID:On the association of glycolytic enzymes with structural proteins of skeletal muscle. 111 88

In this study we compare the specific activities and isoenzyme patterns of five enzymes--phosphoglucose isomerase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and alkaline phosphatase--in term placenta with the analogous enzymes in a clone of choriocarcinoma cells grown in culture. Phosphoglucose isomerase, phosphoglucomutase, and lactate dehydrogenase specific activities of the choriocarcinoma did not differ by more than two or three times from the mean activities of the comparable enzymes in placenta; the specific activity of hexokinase in the choriocarcinoma amounted to 14 per cent of the mean value for placenta. In contrast, the mean specific activity of heat-stable alkaline phosphatase in the choriocarcinoma amounted to only 1 per cent of the mean value for placenta. By growing the cells in 5-bromodeoxyuridine, 20 mug per milliliter, we were able to increase alkaline phosphatase activity to 68 per cent of the mean value for placenta. For both extracts, phosphoglucose isomerase zymograms were similar and phosphoglucomutase zymograms were similar. The hexokinase zymogram of term placenta showed two isoenzymes which stained more intensely with 0.5 mM. glucose than with 0.1M glucose. A hexokinase isoenzyme was observed in zymograms of both extracts which stained more intensely with 0.1M glucose than with 0.5 mM glucose. Lactate dehydrogenase exhibited an extra isoenzyme in the choriocarcinoma extract. When the cells were cultivated in medium containing 5 mug per milliliter of 5-bromodeoxyuridine, the induced phosphatase in the cell line was electrophoretically similar to placental phosphatase. At higher concentrations of 5-bromodeoxyuridine, the most anodal isoenzyme was 0.5 cm. slower in mobility than the comparable placental isoenzyme.
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PMID:Enzymes of normal and malignant trophoblast: phosphoglucose isomerase, phosphoglucomutase, hexokinase, lactate dehydrogenase, and alkaline phosphatase. 111 69

The levels of glycolytic enzymes, aldolase, phosphohexose isomerase and lactic dehydrogenase, the latter as total and isozymes, were determined in the vitreous and aqueous humors and sera as well as in lens-saline extracts of the cat, Rhesus monkey, guinea pig, rabbit, rat and cattle. Although wide species differences were noted, the levels were generally lower in the aqueous as compared to the vitreous and serum. Aldolase and phosphohexose isomerase were invariably elevated in the lens of most species. The LDH isozyme patterns were quite unique in regard to the fluids and the species. The ratios of enzyme contents of the intraocular fluids to the respective sera were calculated and the findings compared. As tested in a few species, no remarkable enzyme differences could be discerned as a result of prior dark or light adaptation of the eyes.
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PMID:Glycolytic enzyme levels of intraocular fluids and lens as compared to the respective sera of various animal species. 112 35

Chromatography of seminal plasma from fresh, untreated chicken semen on Bio-Rad A1.5m agarose gel yielded five major peaks of ultraviolet absorbancy at 280 nm. Two peaks with 280/260 absorbancy ratios less than unity suggested the presence of free nucleotides. Enzyme assays on the eluent fractions resulted in substantial single peaks of lactic dehydrogenase, glutamic oxaloacetic transaminase, phosphohexose isomerase, acid phosphatase and alkaline phosphatase activity. Acetylcholinesterase and aminopeptidase assays produced multiple peaks of activity. No trypsin-like enzyme activity was detected, suggesting the presence of a seminal plasma trypsin-like enzyme inhibitor. Molecular weight estimates were obtained for all enzyme activity peaks.
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PMID:Activity of eight enzymes of chicken seminal plasma in the eluent from agarose gel chromatography. 113 30

The erythrocytes of 350 pigtailed macaques (Macaca nemestrina) were examined for electrophoretic variation of hemoglobin and 26 enzymes. Seven enzymes showed variation in more than 1% of individuals: phosphoglucose isomerase, phosphoglucomutase-1, soluble NADP-dependent isocitric dehydrogenase, peptidase A, peptidase C, 2,3-diphosphoglycerate mutase, and acid phosphatase. Variation with lesser frequency was found in soluble glutamic-oxalacetic transaminase, phosphoglycerate kinase, lactic dehydrogenase, and hemoglobin. Only eight samples were tested for esterase D, and one of these had a variant phenotype. Enzymes with no clear variation were adenylate kinase, adenosine deaminase, phosphofructokinase, hexokinase, pyruvate kinase, glyceraldehyde 3-phosphate dehydrogenase, aldolase, phosphoglycerate mutase, phosphopyruvate hydratase (enolase), phosphoglucomutase-3, and superoxide dismutase. There was father-to-son transmission of PGI, PGM-1, peptidase C, 6PGD, 2,3-DPGAM, NADP-ICD, and acid phosphatase variants, suggesting that these loci are autosomal as in man.
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PMID:Intraspecific red cell enzyme variation in the pigtailed macaque (Macaca nemestrina). 114 87

A method for the biochemical identification of protozoa belonging to the genus Eimeria is described for the first time. Starch gel electrophoresis of the enzymes lactate dehydrogenase, glucose phosphate isomerase, 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase from parasite extracts revealed both intra- and inter-species differences when 11 strains representative of 6 species of Eimeria were examined. Oocysts were the most accessible parasite stage for investigation but sporozoites and merozoites of an embryo-adapted strain of E. tenella were also examined for enzyme activity.
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PMID:Enzyme variation in Eimeria species of the chicken. 120 11

The authors describe simple and rapid separation technics by electrophoresis on cellulose acetate of glucose-6-phosphate dehydrogenase isoenzymes, 6-phosphogluconate dehydrogenase, phosphoglucomutase, adenosine deaminase, adenylate kinase, phosphohexose isomerase, lactate dehydrogenase iosenzymes in the red cells. These technics are derived from those of Rattazi et al. for glucose-6-phosphate dehydrogenase and Sonneborn for 6-phosphogluconate dehycrogenase, phosphoglucomutase, adenosine deaminase, adenylate kinase and acid phosphatase.
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PMID:[Determination of the phenotypes of several erythrocytic enzymes by cellulose acetate electrophoresis]. 122 49

Ehrlich's test, serum mucoproproteins, phosphohexoisomerase (PHI), and lactate dehydrogenase (LDH) levels were studied in patients with cancer and age matched controls. All parameters studied were found to be significantly increased in cancer. Evaluation of Ehrlich's test, PHI and LDH for their validity as screening tests revealed that Ehrlich's test is better suited as a screening test for cancer. A positive correlation observed in the study between serum mucoproteins and Ehrlich's test strengthens the postulation that mucoproteins are responsible for the colour development in Ehrlich's test.
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PMID:Evaluation of Ehrlich's test as screening test for cancer. 129 68


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