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:3.4.15.1 (ACE)
18,300 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Eight enzymes, e.g. lactate dehydrogenase, malate dehydrogenase, fructose-diphosphate aldolase, sorbitol dehydrogenase, glucose-6-phosphate dehydrogenase, hexokinase, phosphofructokinase and pyruvate kinase were estimated quantitatively in the rat lens from 37 to 1,211 days of age, by spectrophotometric methods. The activity was expressed as mU/g LWW. All enzymes measured showed declining activities, but LDH, ALD, SDH, G-6-PDH, HK and PFK gave a significant decrease during ageing when plotted semi-logarithmically from 37 to 1,211 days. SDH and G-6-PDH showed a statistically significant difference between the enzymes from the male and the female lenses. The female lens always had a lower activity than the male lens. Of all enzymes the specific activity, expressed as mU/l mg protein, was calculated. This specific activity appeared to be rather constant during ageing, except for ALD. In the female lenses, the specific activity of 7 enzymes was lower than in the male lenses. For ALD the specific activity decreased significantly in the male lens from 5.32 at 37 days to 0.88 at 1,211 days. In the female lens this significant decrease was from 4.97 to 0.81.
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PMID:The quantification of eight enzymes from the ageing rat lens, with respect to sex differences and special reference to aldolase. 340 13

Ultrastructural, functional, and cytochemical characteristics of resident sinusoidal macrophages (RSM) in brown bullhead (Ictalurus nebulosus) liver were examined. Following perfusion fixation of the hepatic vascular bed, light micrographs revealed RSM that possessed multiple elongate cytoplasmic processes and frequently contained erythrocytes in various stages of degradation. Following brief perfusion fixation, light microscope examination of vibratome sections of bullhead liver reacted for peroxidase revealed intensely positive RSM. By transmission electron microscopy, peroxidase activity was localized to the nuclear envelope and cytoplasmic granules of RSM and in endothelial and perisinusoidal fat-storing cells. In cryostat sections of fresh-frozen liver, glucose-6-phosphate dehydrogenase (G-6-PDH) was uniformly distributed over hepatocytes, whereas intensely positive punctate staining for G-6-PDH was localized over RSM. To test for phagocytosis by RSM, latex beads (0.81 micron) were injected into a tributary of the hepatic portal vein 2 min prior to perfusion fixation. Latex beads appeared either singly or in dense aggregates within RSM. Ultrastructurally, RSM were characterized by an irregularly shaped, eccentrically located nucleus, electron-dense vacuoles, small patches of granular endoplasmic reticulum, a well-developed Golgi apparatus, elongated mitochondria, desmosomes or desmosome-like densities that served as a source of attachment to endothelial cells, and a centriole with radiating microtubules. Invaginations of the plasma membrane (vermiform processes) characteristic of mammalian Kupffer cells were not observed in bullhead RSM. The results indicated a resident cell population of sinusoidal macrophages in the bullhead liver with properties that partially resembled mammalian Kupffer cells. These results are important for the identification of the normal resident cells in the bullhead liver.
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PMID:Resident sinusoidal macrophages in the liver of the brown bullhead (Ictalurus nebulosus): an ultrastructural, functional and cytochemical study. 344 51

The levels of adenosine triphosphate (ATP) in the transplantable CaNT murine tumor grown in CBA mice at various times following 5, 10, and 15 Gy X rays (100 kVp) were increased within 45 min. Maximal ATP levels occurred at 2.5 h following the 10 Gy dose (3.8 times that of unirradiated controls), returning almost to control levels by 13 h after irradiation. The specific activity of glucose-6-phosphate dehydrogenase (G-6-PDH) after 10 Gy increased about 1.5-fold 1 h after irradiation, returning to control levels by 48 h. It is suggested that the increased ATP following irradiation might play a major role in energy provision when cellular repair processes are able to operate. The increased G-6-PDH activity after irradiation may reflect enhanced metabolism associated with cellular repair mechanisms.
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PMID:Effect of X irradiation on adenosine triphosphate and glucose-6-phosphate dehydrogenase in the CaNT mouse tumor. 357 58

The acinar distribution of glutathione S-transferase (GST), glutathione peroxidase (GPx), glutathione reductase (GR), and glucose-6-phosphate dehydrogenase (G-6-PDH) was examined by analyzing periportal (p.p.) and perivenous (p.v.) rat hepatocytes selectively isolated by the digitonin-collagenase perfusion. The cytosolic GST activity was higher in p.v. cells, but the microsomal GST and cytosolic GR were found to be evenly distributed in the acinus. In contrast, the activity of both the Se-dependent GPx and the microsomal (Se-independent) GPx, as well as G-6-PDH, was much lower in the p.v. than in the p.p. cells. The heterogeneous distribution of GST, GPx and G-6-PDH was confirmed by analyzing liver perfusion effluents collected after ante- or retrograde digitonin infusion. The relatively low activities of GPx and G-6-PDH in the p.v. cells could partly explain the susceptibility of this region to chemical injury.
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PMID:Acinar distribution of glutathione-dependent detoxifying enzymes. Low glutathione peroxidase activity in perivenous hepatocytes. 359 5

The role of adaptive hormones and serum lipoproteins in the regulation of glucose-6-phosphate dehydrogenase (G-6-PDH) activity was investigated. The test was performed on experimental hepatic sections of Wistar rats. It was shown that timely regulation of G-6-PDH by epinephrine and hydrocortisone which inhibits the activity of enzyme is manifested through the cAMP-dependent mechanism. The cooperative effect of epinephrine, hydrocortisone and high-density lipoproteins that enables G-6-PDH activation was revealed. It was stated that only high-density lipoproteins of subpopulation III were capable of hormonal mediating. The effect was caused by the induction of enzyme synthesis and manifested through lysosome-dependent activation of chromatin.
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PMID:[Cooperative effect of hydrocortisone, adrenaline and high-density lipoproteins in regulating the glucose-6-phosphate dehydrogenase activity of the liver]. 376 80

Primary roots of soybean [Glycine max (L.), cv Harosoy 63] seedlings were inoculated with zoospores from either race 1 (incompatible, host resistant) or race 3 (compatible, host susceptible) of Phytophthora megasperma f. sp. glycinea (Pmg) and the activities of phenylalanine ammonia-lyase (PAL), chalcone synthase (CHS), isoflavone synthase, and dihydroxypterocarpan 6a-hydroxylase related to phytoalexin (glyceollin) biosynthesis, and of glucose-6-phosphate dehydrogenase (Glc-6-PDH) and glutamate dehydrogenase (Glu-DH) were determined at various times after inoculation. About 2-4 h after inoculation with race 1, the activities of PAL, CHS, and pterocarpan 6a-hydroxylase were higher than after inoculation with race 3 and increased considerably thereafter. In contrast, activities of these enzymes in the compatible interaction were equal to or only slightly higher than in the controls over the entire infection period investigated (2-8 h). Isoflavone synthase did not increase until 7 h after inoculation with race 1. There were no significant differences in activities for Glc-6-PDH and Glu-DH between inoculated roots and controls. The results show that infection of soybean roots with zoospores of Pmg race 1 causes a race:cultivar-specific early induction of enzymes involved in glyceollin synthesis, whereas such an induction does not occur with zoospores of race 3. These findings are in agreement with the race:cultivar-specific accumulation of glyceollin in soybean roots reported previously [M. G. Hahn, A. Bonhoff, and H. Grisebach (1985) Plant Physiol. 77, 591-601].
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PMID:Race:cultivar-specific induction of enzymes related to phytoalexin biosynthesis in soybean roots following infection with Phytophthora megasperma f. sp. glycinea. 396 19

Cytochemistry was used to measure the activity of succinate dehydrogenase (SOD), lactate dehydrogenase (LDH) and glucose-6-phosphate dehydrogenase (G-6-PDH) in rat peritoneal macrophages under the action of the endogenous immunostimulant tuftcin (tre-lys-pro-arg) during phagocytosis of latex particles and at rest. Tuftcin did not affect the activity of the study enzymes in non-phagocytic cells. Elevation of the peptide concentration to 0.25 micrograms/ml and higher in phagocytic macrophages activated G-6-PDH and lowered the activity of LDH. Tuftcin did not alter the activity of SOD in phagocytic macrophages.
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PMID:[Effect of tuftsin on the activity of energy metabolism enzymes in peritoneal macrophages]. 398 36

A single total-body exposure of rats to gamma-rays in an absolutely lethal dose caused significant changes in the activity of fructosodiphosphate aldolase (ALD) and glucose-6-phosphate dehydrogenase (G-6-PDH) in the brain, liver, myocardium and skeletal muscles. The activity of ALD was mainly inhibited and that of G-6-PDH increased. Thus, the initial step of glycolysis was significantly inhibited and the key reaction of the pentose phosphate pathway enhanced in the irradiated body.
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PMID:[Changes in fructosediphosphate aldolase and glucose-6-phosphate dehydrogenase activity after irradiation of animals with an absolute lethal dose of gamma rays]. 400 26

Cathepsins M and B from rabbit liver lysosomes were separated by chromatography on Ultrogel AcA34 at low ionic strength and purified to homogeneity, and their catalytic and molecular properties were compared. Cathepsin M was relatively inactive with synthetic peptide substrates. Thus, it hydrolyzed benzoyl arginine naphthylamide at only one-fifth the rate observed with cathepsin B, and no activity was detected with Gly-Phe naphthylamide which is a relatively good substrate for cathepsin B. On the other hand, cathepsin M exhibited a preference for protein substrates. It was more active than cathepsin B in catalyzing the inactivation of the following enzymes: rabbit muscle or liver fructose-1,6-bisphosphate aldolases, rabbit liver fructose-1,6-bisphosphatase and pyruvate kinase, yeast glucose-6-phosphate dehydrogenase, and rabbit muscle glyceraldehyde-3-phosphate dehydrogenase. With glucagon as substrate, both enzymes showed similar peptidyl dipeptidase activities with some minor differences in peptide bond specificity. Cathepsins M and B are similar in size, with apparent molecular weights of 30,200 for cathepsin M and 28,800 for cathepsin B, and in amino acid composition and carbohydrate content. Each contains approximately 2-3 equivalents/mol glucosamine, 3 equivalents/mol mannose, and no fucose or galactosamine. They also show similar microheterogeneity in sodium dodecylsulfate-gel electrophoresis and isoelectric focusing; this microheterogeneity is probably related to differences in glycosylation. Extensive homology in primary structure for the two proteins was indicated by the similar patterns of peptides formed on digestion with trypsin.
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PMID:Purification and properties of rabbit liver cathepsin M and cathepsin B. 406 7

Ragland, T. E. (Brandeis University, Waltham, Mass.), T. Kawasaki, and J. M. Lowenstein. Comparative aspects of some bacterial dehydrogenases and transhydrogenases. J. Bacteriol. 91:236-244. 1966.-Twenty-eight diverse bacterial species were surveyed for the activities and coenzyme specificities of four enzymes: isocitrate dehydrogenase (ICDH), glucose-6-phosphate dehydrogenase (G-6-PDH), 6-phosphogluconate dehydrogenase (6-PGDH), and reduced nicotinamide adenine dinucleotide phosphate-nicotinamide adenine dinucleotide (NAD) transhydrogenase (TH). Most of the species that exhibited a nicotinamide adenine dinucleotide phosphate (NADP)-linked ICDH also showed significant TH activity, but there were several which did not. Only one of the organisms tested, Xanthomonas pruni, had an ICDH active with both NAD and NADP; it was devoid of TH activity. Acetobacter suboxydans, which lacks ICDH altogether, also had no TH. Some of the species examined had G-6-PDH or 6-PGDH (or both) of dual coenzyme specificity, but there was no apparent relation between these findings and the presence or absence of TH. The TH reaction was assayed by use of analogues of NAD as acceptors. The bacteria could be divided into two groups on the basis of TH specificity, one group reacting at a much faster rate with the 3-acetylpyridine analogue of NAD than with the thionicotinamide analogue, whereas the converse was true for the other group. A few organisms showed no marked specificity for either analogue. This division of specificity can be related to the currently accepted taxonomic classification of the organisms, although a few apparent anomalies were found.
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PMID:Comparative aspects of some bacterial dehydrogenases and transhydrogenases. 437 10


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