Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:4.1.2.13 (aldolase)
 3,461 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Inactivation rates for nine enzymes extracted from Bacillus cereus spores were measured at several temperatures, and the temperature at which each enzyme had a half-life of 10 min (inactivation temperature) was determined. Inactivation temperatures ranged from 47 degrees C for glucose 6-phosphate dehydrogenase to 70 degrees C for leucine dehydrogenase, showing that spore enzymes were not unusually heat stable. Enzymes extracted from vegetative cells of B. cereus had heat stabilities similar to the respective enzymes from spores. When spores were heated and the enzymes were subsequently extracted and assayed, inactivation temperatures for enzymes within the spore ranged from 86 degrees C for glucose 6-phosphate dehydrogenase to 96 degrees C for aldolase. The internal environment of the spore raised the inactivation temperature of most enzymes by approximately 38 degrees C. Loss of dipicolinic acid from spores was initially slow compared with enzyme inactivation but increased rapidly with longer heating. Viability loss was faster than loss of most enzyme activities and faster than dipicolinic acid release.
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PMID:Heat stability of Bacillus cereus enzymes within spores and in extracts. 677 28

The electrophoretic mobilities of seven enzymes from eight theileria-infected bovine lymphoblastoid cell lines originating in Kenya and Iran were compared. The isoenzyme patterns of phosphoglucomutase, malate dehydrogenase, malic enzyme and glucose-6-phosphate dehydrogenase were the same for all cell lines infected with any of the three Theileria species. Theileria annulata could be clearly differentiated from T parva and T lawrencei on the basis of three enzymes: glucose phosphate isomerase, glyceraldehyde phosphate dehydrogenase and aldolase. T parva and T lawrencei isoenzyme patterns were alike except for glucose phosphate isomerase, where two sets of isoenzyme mobility were shown which, however, did not separate the two species.
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PMID:Preliminary investigations on isoenzyme variants of lymphoblastoid cell lines infected wih Theileria species. 678 78

Oral administration of lantana leaf powder to guinea pigs caused an increase in the hepatic postmitochondrial fraction:homogenate ratios of activities of lysosomal enzymes--acid phosphatase, cathepsin B and DNase II. Enzyme activities of glucokinase, aldolase, lactate dehydrogenase and glucose-6-phosphate dehydrogenase were elevated whereas activity of glutathione-S-transferase decreased. Alterations in the activities of lysosomal and cytosol enzymes appear to constitute an important biochemical lesion in the pathogenesis of guinea pig liver in lantana toxicity.
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PMID:Effect of lantana toxicity on lysosomal and cytosol enzymes in guinea pig liver. 683 12

The sequence of inactivation of five bovine erythrocyte enzymes (glucose-6-phosphate dehydrogenase, pyruvate kinase, lactate dehydrogenase, aspartate aminotransferase and aldolase) was compared during in vivo aging of the red blood cell and during treatment of the cells with heat, gamma-radiation and an enzymatic source of the superoxide radical anion. Amounts of oxygen free radicals comparable to those formed physiologically in the cells were able to induce considerable inactivation of some enzymes; in no case was the physiological sequence of inactivation reproduced. These results seem to argue for a multifactorial inactivation of red cell enzymes during intravascular aging of the erythrocyte.
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PMID:Aging of the erythrocyte. VII. On the possible causes of inactivation of red cell enzymes. 689 33

Clones of 32 strains of Trichomonas vaginalis isolated from patients attending a venereal diseases clinic were compared among themselves and with authentic Pentatrichomonas hominis on the basis of their isoenzyme patterns for eight enzymes by thin-layer starch-gel electrophoresis. The enzymes examined were: glucose phosphate isomerase (GPI); phosphoglucomutase (PGM); malic enzyme (NADP+) (ME); hexokinase (HK); malate dehydrogenase (NAD+) (MDH); glucose-6-phosphate dehydrogenase (G6PD); aldolase (ALD); and lactate dehydrogenase (LDH). From the isoenzyme patterns of four enzymes (LDH, MDH, HK, and GPI) the strains of T vaginalis could be divided clearly into five groups. PGM showed differences in only one strain, while two other enzyme patterns (ME and ALD) were the same for all the strains of T vaginalis tested. All isolates were clearly distinguishable from P hominis. Although G6PD patterns were not sharp some differences were evident among T vaginalis strains.
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PMID:Isoenzyme characterisation of Trichomonas vaginalis. 698 Jun 85

The effect of 90% jejunoileal bypass procedure on liver enzymes was evaluated in 11 obese Zucker fat rats after a 50% weight loss. Control tissues were also collected from 11 unoperated obese rats. In the jejunoileal bypass group, there was a significant decrease in phosphofructokinase, pyruvate kinase, and glucose-6-phosphate dehydrogenase activities. Pyruvate carboxylase, alanine aminotransferase, and lactate dehydrogenase activities were not altered. Fructose 1,6-biphosphatase, aldolase, aspartate aminotransferase, and phosphoenolpyruvate carboxykinase activities were increased in the jejunoileal bypass group. These studies suggest that after jejunoileal bypass glycolysis is reduced and gluconeogenesis is increased. Amino acids may provide an essential energy source for hepatic function.
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PMID:Changes in hepatic carbohydrate metabolism after jejunoileal bypass. 707 18

Male, Sprague-Dawley rats were weaned prematurely (postnatal day 17) to a starch-based diet. At the age of 182 days, half of the rats were fed for 14 days a diet in which sucrose supplied 40% of the energy. Early weaning led to increases in the activities of hepatic glucose-6-phosphate dehydrogenase (G6PD) and malic enzyme (ME). Compared with spontaneously weaned rats, prematurely weaned animals also showed increases in hepatic lipogenesis in vivo and in liver cholesterol levels. However, early weaning did not influence intraperitoneal glucose tolerance, plasma cholesterol concentrations or the activities of hepatic ketohexokinase (KHK), fructose-1-phosphate aldolase (FIPA) and triokinase (TK). Sucrose feeding led to deterioration of glucose tolerance and to enhanced hepatic lipogenesis in vivo. Sucrose-fed rats also showed increases in the total activities of hepatic G6PD, ME, KHK, FIPA and TK. There was a positive interaction in effects on liver size between early weaning and dietary sucrose. In general, however, there were no differences between prematurely and normally weaned rats in their responses to sucrose. The results did not support the idea that dietary adaptations in early life alter the manner in which adult rats respond to dietary stimuli.
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PMID:Effects of premature weaning on the metabolic response to dietary sucrose in adult rats. 707 28

The energy metabolism of the English E-CMO strain of contagious equine metritis bacterium was studied in whole cells and cell extracts. This bacterium appears to have an active Krebs cycle and probably obtains energy by oxidative phosphorylation since glycolysis and the hexose monophosphate pathways appear to be absent. These conclusions are based on the findings that [U-14C]glucose incorporation by this bacterium is below the level of detection, and that respiration is stimulated by Krebs cycle intermediates (i.e., malate, citrate, and succinate), but not by glucose, fructose, maltose, or sucrose. Furthermore, support comes from the fact that enzymes generally associated with the Krebs cycle and electron transport (i.e., malate dehydrogenase, succinate dehydrogenase, isocitrate dehydrogenase, fumarate hydratase, malate dehydrogenase [decarboxylating], cytochrome oxidase, superoxide dismutase, NADH dehydrogenase, and catalase) were detected. Those enzymes normally associated with glycolysis and the hexose monophosphate pathways (i.e., hexokinase, glucose 6-phosphate dehydrogenase, fructose biphosphate aldolase, glycerol 3-phosphate dehydrogenase, phosphoenolpyruvate carboxykinase, pyruvate kinase, phosphate acetyl transferase, acetate kinase, alcohol dehydrogenase, and lactate dehydrogenase) were below the level of detection.
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PMID:Energy metabolism of the contagious equine metritis bacterium. 708 71

Stability of lactatedehydrogenase (LDG) and glucose-6-phosphate dehydrogenase (G-6-PhDG) to the action of heating and urea on the muscle and on the enzymes isolated from muscle was studied. By the stability to the thermal agent in the system of the muscle and out of it LDG and G-6-PhDG exceed creatine kinase and aldolase; the most thermostable enzyme is G-6-PhDG. According to the action of urea on the muscle G-6-PhDG is the most stable enzyme, LDG is the most labile one among the studied enzymes. Under the action of urea on the isolated enzymes G-6-PhDG is the most labile one.
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PMID:[Effect of urea and heating on lactate dehydrogenase and glucose-6-phosphate dehydrogenase activity]. 709 15

In extracts of adult Angiostrongylus cantonensis, the activities of enzymes including glucokinase, phosphoglucoisomerase, phosphofructokinase, aldolase, triosepho sphate isomerase, glyceraldehydephosphate dehydrogenase, phosphoglycerokinase, phosphoglyceromutase, enolase, pyruvate kinase, lactate dehydrogenase, pyruvate decarboxylase, alcohol dehydrogenase, glucose 6-phosphate dehydrogenase, glycerophosphate dehydrogenase and pyruvate dehydrogenase complex were demonstrated. The present of significant activity of glycerophosphate dehydrogenase and glucose 6-phosphate dehydrogenase may indicate the possibility of an operative of alpha-glycerophosphate and pentose phosphate pathway.
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PMID:Glycolytic enzymes in juvenile and adult Angiostrongylus cantonensis. 711 11


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