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:1.4.1.2 (glutamate dehydrogenase)
4,380 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Use of the gel film technique in microphotometric determinations of enzyme activity is described. The microscope photometer is computer-controlled. It is programmed to deal with repetitive measurements at up to 12 selected positions within a tissue section and to evaluate recorded reaction rates statistically. Films of polyacrylamide gel with entrapped glucose-6-phosphate dehydrogenase are used as a model to demonstrate the correlation between local enzyme activity and the microphotometrically determined reaction rate. Enzyme activities at different positions in the same tissue section are determined and compared. Activity profiles of five enzymes (glutamate dehydrogenase, lactate dehydrogenase, malate dehydrogenase, succinate dehydrogenase, NAD-dependent tetrazolium reductase) in the liver are presented and show non-uniform intra-acinar distribution patterns. These results are interpreted in the light of the metabolic zonation of the hepatic acinus. Further applications of the method are discussed.
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PMID:Microphotometric determination of enzyme activities in cryostat sections by the gel film technique. 26 70

Isolated membrane fractions of Escherichia coli K-12 yielded complex immunoprecipitate patterns when Triton X-100 and sodium dodecyl sulfate extracts were examined by crossed immunoelectrophoresis with antienvelope immunoglobulins. Twelve of the 46 antigens in the immunoprecipitate patterns of inner (plasma) membranes were identified by zymograms and/or by the use of specific antisera. The following enzyme activities were detected in immunoprecipitates: 6-phosphogluconate dehydrogenase (EC 1.1.1.43); adenosine triphosphatase (EC 3.6.1.3); glutamate dehydrogenase (EC 1.4.1.4), two separate components; malate dehydrogenase (EC 1.1.1.37); dihydroorotate dehydrogenase (EC 1.3.3.1); succinate dehydrogenase (EC 1.3.99.1); lactate dehydrogeanse (EC 1.1.1.27); reduced nicotinamide adenine dinucleotide dehydrogenase (EC 1.6.99.3); protease (EC 3.4.21.1); and glycerol 3-phosphate dehydrogenase (EC 1.1.99.5). The corresponding immunoprecipitate pattern for isolated outer membranes consisted of at least 25 discrete antigens and differed strikingly from that obtained with inner membranes. Two major immunogens were identified as lipopolysaccharide and Braun lipoprotein. A protease-active immunoprecipitate was also detected in this fraction, but attempts to identify the Rosenbusch matrix protein in the crossed immunoelectrophoretic profile were unsuccessful.
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PMID:Immunochemical analysis of inner and outer membranes of Escherichia coli by crossed immunoelectrophoresis. 33 83

Yeast mutant lacking proteinase B activity have been isolated [Wolf, D. H. and Ehmann, C. (1978) FEBS Lett. 92, 121--124]. One of these mutants (HP232) is characterized in detail. Absence of the vacuolar localized enzyme is confirmed by checking for proteinase B activity in isolated mutant vacuoles. Defective proteinase B activity segregates 2:2 in meiotic tetrads. The mutation is shown to be recessive. Mutant proteinase B activity is not only absent against the synthetic substrate. Azocoll, but also against the physiological substrate pre-chitin synthetase, cytoplasmic malate dehydrogenase and fructose-1,6-bisphosphatase. The mutant shows normal vegetative growth, a phenomenon not consistent with the idea that proteinase B might be the activating principle of chitin synthetase zymogen in vivo. Fluorescence microscopy shows normal chitin insertion. Enzymes underlying carbon-catabolite inactivation in wild-type cells (a mechanism proposed to be possibly triggered by proteinase B) such as cytoplasmic malate dehydrogenase, fructose-1,6-bisphosphatase, phosphoenolpyruvate carboxykinase and isocitrate lyase, are inactivated also in the mutant. NADP-dependent glutamate dehydrogenase, which is found to be inactivated in glucose-starved wild-type cells, proceeds normally in the mutant. Mutant cells show more than 40% reduced protein degradation under starvation conditions. Sporulating diploids, homozygous for proteinase B absence, also exhibit an approximately 40% reduced protein degradation as compared to homozygous wild-type diploids or diploids heterozygous for the mutant gene. The time of the appearance of the first ascospores of diploid cells, homozygous for proteinase B deficiency, is delayed about 50% and sporulation frequency is reduced to about the same extent as compared to homozygous wild-type diploids or diploids heterozygous for the mutant gene.
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PMID:Studies on a proteinase B mutant of yeast. 38 14

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.
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PMID:Biochemistry of intraerythrocytic parasites. I. Identification of enzymes of parasite origin by starch-gel electrophoresis. 38 67

The effect of toluene on Escherichia coli has been examined. In the presence of Mg2+, toluene removes very little protein, phospholipid, or lipopolysacharide from E. coli. In the absence of Mg2+, or in the presence of EDTA, toluene removes considerably more cell material, including several specific cytoplasmic proteins such as malate dehydrogenase (EC 1.1.1.37). In contrast, glucose-6-phosphate dehydrogenase (EC 1.1.1.49) and glutamate dehydrogenase (EC 1.4.1.4) are not released at all under the same conditions. Cells treated with toluene in the presence of Mg2+ remain relatively impermeable to pyridne nucleotides, while cells treated with toluene in the presence of EDTA become permeable to these compounds. Freeze-fracture electron microscopy shows that toluene causes considerable damage to the cytoplasmic membrane, while the outer membrane remains relatively intact. These results indicate that the permeability characteristics of toluene-treated cells depend at least partly on the state of the outer membrane after the toluene treatment.
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PMID:The effect of toluene on the structure and permeability of the outer and cytoplasmic membranes of Escherichia coli. 41 78

Six strains of Rickettsia prowazekii, two derived from human infections and four isolated from flying squirrels, two strains of R. typhi, and the single available strain of R. canada, were characterized by several biochemical procedures. The electrophoretic patterns on polyacrylamide gels of rickettsial proteins solubilized by sodium dodecyl sulfate revealed several species differences, but strains of the same species appeared to have identical patterns. Cytoplasmic fractions of the rickettsiae were examined for enzymatic activities and for polyacrylamide gel isoelectric focusing patterns. Some species differences were encountered in the activities or ratios of activities of glutamate-oxaloacetate transaminase, glutamate dehydrogenase, and malate dehydrogenase. When polyacrylamide gels were stained for malate dehydrogenase after electrophoresis, a single band became apparent with single extracts or mixtures of two strains of R. prowazekii, but two bands were seen with mixtures of a strain of R. prowazekii and one of R. typhi. The isoelectric focusing patterns of the soluble proteins revealed numerous species differences, especially between R. canada and the other two species, and a few differences among the strains of R. prowazekii. The patterns of the two human strains, Breinl and E(R), differed in at least one location, and both differed from the flying squirrel strains in the displacement of one band. One of the flying squirrel strains, GvF-16, contained a protein band not seen in the other five strains. Despite these minor differences, a striking similarity was revealed by all the biochemical tests performed between the R. prowazekii strains of human and flying squirrel origin.
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PMID:Biochemical characteristics of typhus group rickettsiae with special attention to the Rickettsia prowazekii strains isolated from flying squirrels. 41 82

NAD- and NADP-dependent dehydrogenases in gastric adenocarcinoma and undifferentiated cancer cells were studied comparatively. The activity of NADP-dependent malate dehydrogenase, glutamate dehydrogenase and glucose-6-phosphate dehydrogenase was found to be high in gastric adenocarcinoma, while there was noted a more high activity of succinate dehydrogenase and NAD-dependent malate dehydrogenase in undifferentiated cancer. Differences ni the activity of oxido-reductive enzymes in adrenocarcinoma and undifferentiated cancer are discussed from the standpoint of various histogenesis of these forms of gastric cancer.
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PMID:[Oxidoreductase activity in the cells of stomach cancer]. 48 98

Intraacinar distribution of succinate dehydrogenase (SDH), malate dehydrogenase (MDH), NADP-dependent isocitrate dehydrogenase (IDH), glutamate dehydrogenase (GluDH), lactate dehydrogenase (LDH) and NADH-tetrazolium dehydrogenase (TR) was studied in rat liver cryostat sections by multipositional microphotometric activity determinations. By statistical evaluation, activity of individual enzymes could be related to the acinar topography. Activity was evaluated with regard to distance of measuring position either from afferent (portal) or efferent (hepatic) vessels. Two independent distribution curves were obtained for each enzyme. Acinar distribution of all the enzymes studied followed sigmoid courses with maximal activity of SDH, MDH and LDH in zone 1 ("periportal") and GluDH, IDH, TR in zone 3 ("pericentral"). For all enzymes, maximum activity gradients were confined to zone 2 of the acinus. Data were also evaluated as ratios of activities in zone 1 and zone 3. The following ratios zone 1/zone 3 were obtained: SDH = 1.9, MDH = 1.7, IDH = 0.5, GluDH = 0.5, LDH = 1.3 and TR = 0.6.
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PMID:Microphotometric studies on intraacinar enzyme distribution in rat liver. 52 13

1. The presence of glutamate dehydrogenase in the microsomal fraction of rat liver was confirmed. The identities of mitochondrial and microsomal glutamate dehydrogenases were proved by immunochemical methods and by SDS polyacrylamide gel electrophoresis of purified enzymes. 2. Synthesis of glutamate dehydrogenase by the membrane-bound ribosomes of rough endoplasmic reticulum was determined. Newly synthesized enzyme molecules were discharged on the cytoplasmic surface of endoplasmic reticulum membranes. 3. A precursor-product relationship was found between microsomal and mitochondrial glutamate dehydrogenases. About six hours were needed for the transport of glutamate dehydrogenase from the site of synthesis to mitochondria. 4. The half-life of glutamate dehydrogenase was about 5.5 days, which was somewhat longer than that of mitochondrial total protein determined in the same experiment. 5. Mitochondrial-type malate dehydrogenase was also present in the microsomal fraction. Subfractionation of smooth microsomes revealed the existence of particular light microsomal vesicles in which both glutamate dehydrogenase and malate dehydrogenase were concentrated. These vesicles may participate in intracellular transport of matrix enzymes from microsomes to mitochondria.
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PMID:Biogenesis of the mitochondrial matrix enzyme, glutamate dehydrogenase, in rat liver cells. I. Subcellular localization, biosynthesis, and intracellular translocation of glutamate dehydrogenase. 59 7

1. Glutamate dehydrogenase and malate dehydrogenase solubilized from liver microsomes were able to rebind to microsomal vesicles while the corresponding dehydrogenases extracted from mitochondria showed no affinity for microsomes. 2. Competition was noticed between microsomal glutamate dehydrogenase and microsomal malate dehydrogenase in the binding to microsomal membranes. Mitochondrial malate dehydrogenase or bovine serum albumin did not inhibit the binding of microsomal glutamate dehydrogenase to microsomes. 3. Binding of microsomal glutamate dehydrogenase to microsomal membranes decreased when microsomes was preincubated with trypsin. 4. Rough microsomal glutamate dehydrogenase was more efficiently bound to rough microsomes than smooth microsomes. Conversely, smooth microsomal glutamate dehydrogenase had higher affinity for smooth microsomes than for rough microsomes. 5. A difference was noticed among the glutamate dehydrogenase isolated from rough and smooth microsomes, and from mitochondria, which suggested the possibility of minor post-translational modification of enzyme molecules in the transport from the site of synthesis to mitochondria.
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PMID:Biogenesis of the mitochondrial matrix enzyme, glutamate dehydrogenase, in rat liver cells. II. Significance of binding of glutamate dehydrogenase to microsomal membrane. 59 8


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