Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.3.5.1 (succinate dehydrogenase)
 8,177 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of unilateral nephrectomy (UN) and streptozotocin (STZ) diabetes on the activities of enzymes involved in uridine and cytidine synthesis in early renal growth (3-14 days after stimulus to growth) have been compared. Measurements were also made of glucose-6-phosphate dehydrogenase (G6PDH) and 6-phosphogluconate dehydrogenase (6PGDH) and of glucose 6-phosphate (G6P), UDP-glucose, and glycogen, in relation to phosphoribosyl pyrophosphate, ribonucleotide, and complex carbohydrate formation. There were striking differences in the activities of CTP synthetase, G6PDH, and 6PGDH in the two conditions, with a three-fold increase in all three enzymes at 3 and 5 days and a two-fold increase above basal values at 14 days of STZ diabetes. The UN group showed no significant change in CTP synthetase at any stage and the activity of G6PDH and 6PGDH only kept pace with renal growth. Changes in routes of uridine synthesis were less marked, with a more rapid rise in carbamoyl-phosphate synthetase (glutamine) and a lesser response of dihydroorotate dehydrogenase in the UN relative to the STZ-diabetic groups. The enzymes of complex II and of uracil phosphoribosyltransferase showed essentially similar patterns during renal hypertrophy in UN and STZ diabetes. The parallel increase in CTP synthetase, G6PDH, and 6PGDH in the kidney in diabetes, also known to increase in growth situations in hepatomas and in renal tumors, is discussed in relation to hormone signals involved in renal growth. The importance of the concentration of CTP, and thus of CTP synthetase, in the CTP-cytidyltransferase reaction, an enzyme with a high Km for CTP, makes the present observation of the striking increase in CTP synthetase in STZ diabetes of particular interest in relation to phosphatidylcholine formation and hormone signal transduction.
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PMID:Uridine and cytidine nucleotide synthesis in renal hypertrophy: biochemical differences in response to the growth stimulus of diabetes and unilateral nephrectomy. 138 Dec

The metabolic functions of endothelial cells of the rabbit cornea in different storage conditions were studied using quantitative cytochemistry. The corneas were stored for 2 h, and 1, 3, 7, 14 and 21 days in dexol at 4 degrees C and in culture medium at 37 degrees C. It was shown that glycolysis as expressed by the activity of the cytosolic enzymes glyceraldehyde 3-phosphate dehydrogenase, glucose-6-phosphate dehydrogenase and lactic dehydrogenase is well preserved for 1 week in dexol and for 3 days only in the culture medium. Mitochondrial enzymes as shown by succinate dehydrogenase and fatty acid oxidation activity show a similar pattern. Uridine diphosphoglucose dehydrogenase, which plays an important part in proteoglycan synthesis, is markedly decreased in both media, but retains its activity in dexol for a slightly longer time. Keratan and chondroitin sulfate content show a sharp drop in the culture medium at 37 degrees C as compared to dexol. This study demonstrates the superiority of dexol at 4 degrees C over the culture medium at 37 degrees C. Quantitative cytochemistry is a useful tool for studying the metabolism of endothelial cells.
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PMID:Endothelial cells of rabbit cornea in different storage conditions. A quantitative cytochemical study. 187 Aug 47

This paper describes a method for separating and isolating plasma membranes from the septated fungus Podospora anserina. Plasma membranes were isolated from protoplasts (young cell plasma membranes) and mycelia (both young and aged cell plasma membranes). The procedure of fractionation consisted of a combination of differential and isopycnic centrifugations. Characterization of cellular membranes and enrichment of the fractions with plasmalemma were carried out by assays on enzymatic activities. A plasma membrane fraction was isolated in a buoyant density peak of 1.087 g/cm3, where three enzymatic activities bound to plasma membrane, adenylate cyclase, chitin synthase, and beta-glucan synthase at low affinity for UDP-Glc, peaked together. Good purity of this fraction was determined by the absence or the very low level of other enzymatic activities used as markers for intracellular membranes, i.e., succinate dehydrogenase, alpha-mannosidase, NADPH cytochrome c reductase, and beta-glucan synthase at high affinity for UDP-Glc activities.
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PMID:Isolation and characterization of plasma membranes from the fungus Podospora anserina. 621 78