Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.37 (malate dehydrogenase)
 4,591 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Isoelectric focusing studies on enzyme variation between populations of the snail Bulinus senegalensis revealed that parasitic infections in the snails contributed additional bands of enzyme activity, particularly in the glucose phosphate isomerase (GPI) and malate dehydrogenase (MDH) systems. The patterns due to the parasite enzymes were, in most cases, clearly distinct from those of the host and different from each other. Parasites encountered included Schistosoma haematobium, S. bovis, Paramphistomum microbothrium, another amphistome probably belonging to the group which infect amphibians, Echinostoma revolutum, another echinostome (probably Echinoparyphium sp.), strigeids, xiphidiocercariae (these were resolved into 3 distinct types by the enzyme data) and ciliate protozoa. The 7 host populations which were examined showed marked differences in both the prevalence and variety of their parasitic infections and these variations were tentatively related to environmental differences in their respective habitats and to the nature of human contact patterns. Seasonal changes in the parasite fauna were also noted and some of the implications of the parasite load on the host population are briefly mentioned.
 ...
PMID:Parasites in Bulinus senegalensis (Mollusca: Planorbidae) and their detection. 4 58

26 specimens of Presbytis entellus were examined for a variety of blood proteins. In contrast to previous studies of other species of leaf monkeys, our P.entellus sample proved to be very heterogeneous. Polymorphisms were found in the third component of complement, group-specific component, glycine-rich beta-glycoprotein, alpha1-antitrypsin, phosphoglucomutase, 6-phosphogluconate dehydrogenase, adenylate kinase, superoxide dismutase, malate dehydrogenase, and phosphohexose isomerase. Variable band strengths that might represent polymorphism were found in acid phosphatase and lactate dehydrogenase. Further analyses of the P. cristatus sample studied by Barnicot and Hewett-Emmett failed to disclose variation. The interpretation of blood protein variability in relation to sample collection and population structure is discussed.
 ...
PMID:Protein polymorphism in the Hanuman langur (Presbytis entellus). 5 13

For the characterization of null mutants identified in Drosophila populations, several Drosophila enzymes including alcohol dehydrogenase, cytoplasmic malate dehydrogenase, alpha-glycerol phosphate dehydrogenase, and phosphoglucose isomerase were co-purified to homogeneity using an 8-(6-aminohexyl)-amino-ATP-Sepharose affinity column followed by DEAE-Sepharose column chromatography. Mitochondrial malate dehydrogenase was purified by the use of CM-Sepharose and the same ATP affinity column. Alcohol dehydrogenase and alpha-glycerol phosphate dehydrogenase were mapped on a two-dimensional gel. Antiserum was raised in rabbits against these Drosophila enzymes. The presence of cross-reacting material in null mutants was characterized by double immunodiffusion, immunoelectrophoresis, and two-dimensional gel electrophoresis. By immunological techniques, two natural null variants of malic enzyme and one of phosphoglucose isomerase were shown to be negative to cross-reacting material. Two low-dose-rate gamma-radiation-induced null mutants of cytoplasmic malate dehydrogenase were shown to be positive to cross-reacting material. Two-dimensional gel analyses enabled the characterization of three natural null variants of alpha-glycerol phosphate dehydrogenase. The viability of some null mutants with homozygous null or null/deficiency genotypes is discussed in terms of the in vivo metabolic roles of the related enzymes.
 ...
PMID:Biochemical analyses of natural and induced null variants of Drosophila enzymes. 10 48

An ultramicrochemical technique has been adapted to the evolution of enzyme profiles within individual human mammary tumors. Tandem observation of adjacent stained and lyophilized sections permitted dissection of microgram quantities of freeze-dried material within confirmed regions of malignancy. Enzymes frequently monitored to examine glycolytic, respiratory, and metastatic capacity were microanalyzed successfully: lactic dehydrogenase (LDH), phosphoglucose isomerase (PGI), malate dehydrogenase (MDH), acid phosphatase (AP), aldolase (ALD), glucose-6-phosphate dehydrogenase (G6PDH), pyruvate kinase (PK), alpha-glycerophosphate dehydrogenase (alpha-GOPDH), hexokinase (HK), and phosphofructokinase (PRK). All enzyme activities were higher in infiltrating ductal carcinomas than in fibroadenomas. Extracts of tumor cells mixed in varying proportions with brain or muscle extracts of rat evidenced no modification of expected activity. The technical adaptation described provided a sensitive methodology to resolve problems of relication, profile analysis, sample quantity, and selectivity within heterogeneous tissues.
 ...
PMID:Application of a microchemical technique to the elucidation of enzyme activity profiles within single human mammary tumors. 20 41

Enzymes of parasite origin were identified by starch-gel electrophoresis. The species of parasite studied were Plasmodium berghei, Plasmodium yoelii nigeriensis, Babesia rodhaini and Anthemosoma garnhami. Lactate dehydrogenase, glucose phosphate isomerase and (NADP) glutamate dehydrogenase were detected in all species; phosphogluconate dehydrogenase was detected in both Plasmodium species but malate dehydrogenase only in P. y. nigeriensis. Glucose-6-phosphate dehydrogenase, alanine aminotransferase and aspartate aminotransferase were not detected in any parasite.
 ...
PMID:Biochemistry of intraerythrocytic parasites. I. Identification of enzymes of parasite origin by starch-gel electrophoresis. 38 67

Phenotype and gene frequencies are presented for eight polymorphic systems among the Nubians of South Egypt, namely, acid phosphatase, glucose-6-phosphate dehydrogenase, adenylate kinase, 6-phosphogluconate dehydrogenase, esterase D, phosphoglucomutase I, peptidase A, and haptoglobin. Eleven systems, namely, albumin, ceruloplasmin, hemoglobin, lactate dehydrogenase, isocitrate dehydrogenase, phosphohexose isomerase, malate dehydrogenase, peptidase B and C, phosphoglucomutase II, and transferrin were found to be monomorphic. A single electrophoretic variant of phosphohexose isomerase were observed.
 ...
PMID:The Nubians of Kom Ombo: serum and red cell protein types. 61 20

Cell-free extracts of Rickettsia typhi were tested for activities of enzymes of the tricarboxylic acid cycle, of glutamate catabolism, and of glycolysis. The organisms were grown in the yolk sacs of chicken embryos, harvested shortly before the time of embryo death, purified by Renografin density gradient centrifugation, and ruptured in a French pressure cell. The following enzymatic activities were demonstrated: high levels of malate dehydrogenase (MDH), moderate levels of glutamate-oxaloacetate transaminase, glutamate, succinate, and isocitrate dehydrogenases, and citrate synthase, and low levels of glutamate-pyruvate transaminase. The specific activities of some of these enzymes were higher when the rickettsiae were harvested at a time of active proliferation, 3 to 4 days prior to embryo death. Rickettsial MDH was differentiated from host MDH by its migration pattern on polyacrylamide gel electrophoresis. The activities of MDH and two other dehydrogenases, demonstrable after the cells had been disrupted, were absent from purified, intact rickettsial preparations. No activity was detected for glucose-6-phosphate, 6-phosphogluconate, glyceraldehyde-3-phosphate, lactate dehydrogenases, phosphoglucose isomerase, fructoaldolase, or pyruvate kinase. Our results suggest that extracts of R. typhi that contain demonstrable enzymes involved in the catabolism of glutamate and tricarboxylic acid cycle intermediates, unlike Coxiella burnetti, lack detectable glycolytic activity.
 ...
PMID:Enzymatic activities of cell-free extracts of Rickettsia typhi. 82 Jun 44

Setaria cervi, the filarial parasite inhabiting the Indian water buffalo (Bubalus bubalis Linn.) contained almost all the enzymes involved in glycogen degradation. Significant activities of glycogen phosphorylase, glucokinase, phosphoglucomutase, phosphoglucose isomerase, phosphofructokinase, FDP-aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphopyruvate hydratase, pyruvate kinase, lactate dehydrogenase glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase were detected in cell-free extracts of whole worms. The presence of PEP-carboxykinase, malate dehydrogenase, fumarase and fumarate reductase revealed the functioning of the PEP-succinate pathway in addition to phosphorylating glycolysis and pentose phosphate pathway in the parasite. Excepting fumarate reductase all other enzymes were localized in the particulate-free cytosol fraction, although small amounts of glycogen phosphorylase, aldolase and lactate dehydrogenase were also detected in the mitochondrial fraction.
 ...
PMID:Setaria cervi: enzymes of glycolysis and PEP-succinate pathway. 86 May 72

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.
 ...
PMID:Enzymes of carbohydrate metabolism in four human species of Leishmania: a comparative survey. 100 46

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.
 ...
PMID:On the association of glycolytic enzymes with structural proteins of skeletal muscle. 111 88


1 2 3 4 5 6 7 8 9 10 Next >>