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)

The development of key enzyme activities concerned with glucose metabolism was studied in six regions of the rat brain in animals from just before birth (-2 days) through the neonatal and suckling period until adulthood (60 days old). The brain regions studied were the cerebellum, medulla oblongata and pons, hypothalamus, striatum, mid-brain and cortex. The enzymes whose developmental patterns were investigated were hexokinase (EC 2.7.1.1), aldolase (EC 4.1.2.13), lactate dehydrogenase (EC 1.1.1.27) and glucose-6-phosphate dehydrogenase (EC 1.1.1.49). Hexokinase, aldolase and lactate dehydrogenase activities develop as a single cluster in all the regions studied, although the timing of this development varies from region to region. Glucose-6-phosphate dehydrogenase activity, however, declines relative to glycolytic enzyme activity as the brain matures. When the different brain regions are compared, it is clear that the medulla develops its glycolytic potential, as indicated by its potential enzyme activity, considerably earlier than the other regions (hypothalamus, striatum and mid-brain), with the cortex and cerebellar activities developing even later. This enzyme developmental sequence correlates well with the neurophylogenetic development of the brain and adds support to the hypothesis that the development of the potential for glycolysis in the brain is a necessary prerequisite for the development of neurological competence.
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PMID:Regional enzyme development in rat brain. Enzymes associated with glucose utilization. 671 9

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

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

The distribution of enzymes in the blastoderm and the yolk was investigated in the eggs of the bony fish, Misgurnus fossilis. The total activities of lactate dehydrogenase (LDH), glucose-6-phosphate dehydrogenase (G-6-PD), and aldolase (ALD) did not change during early development. However, the enzymes were redistributed in the egg: at the blastula stage the blastoderm contains about 60% of the total ALD activity and 80% of the total LDH and G-6-PD activities. The "free cytoplasm" volume, in which the enzymic proteins can be solubilized, is greater in the yolk than in the blastoderm. Low levels of homologous enzymes from other species injected into the egg are distributed between the blastoderm and the yolk in the same way as are the native enzymes; they are primarily localized in the blastoderm. Injected exogenous enzyme concentrates preferentially in the yolk, apparently being distributed proportionately with respect to the "free cytoplasm" volumes. The ratio of these "free cytoplasmic" volumes, determined by distribution of the injected enzyme (LDH), in the yolk and in the blastoderm is 6.8. On the basis of our results we propose that many egg enzymes are noncovalently bound to blastoderm structures, and that the "nonbound" fraction of the enzymes in the cytosol is distributed proportionally to the "free cytoplasm" volumes in the blastoderm and in the yolk. Fractionation of the subcellular constituents of blastoderm extracts by ultracentrifugation or by gel filtration on Sepharose in the presence of an excess of LDH reveals the high-molecular weight LDH-containing complexes. These complexes are absent in the yolk and in the unfertilized eggs. These results are consistent with the hypothesis that the binding of the enzyme to subcellular structures in the blastoderm is an important mechanism in ooplasmic segregation.
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PMID:Nonuniform distribution of enzymes in fish eggs. 713 Sep 26

Alkaloid biogenesis in Claviceps sp. SD-58 was found to be associated with low growth and reduced consumption of sucrose and mannitol. The activities of glucose-6-phosphate dehydrogenase and aldolase increased up to 9 d of the fermentation cycle and then declined. A close parallel between the operation of pentose phosphate and glycolytic pathways and tryptophan content was demonstrated. An inverse relation between the operation of citric acid and glyoxylate cycles and the ability of the cells to synthesize alkaloids was noted. The role of carbon metabolic pathways during fermentative production of alkaloids is discussed.
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PMID:Activities of catabolic pathways and alkaloid biogenesis during submerged cultivation of Claviceps sp. SD-58. 714 27


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