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)

Red cell enzymes of three children with transient erythroblastopenia of childhood were measured and compared with those of age-matched normal children and children with hemolytic anemia. While the activity of "age-dependent" enzyme such as hexokinase, aldolase, glucose-6-phosphate dehydrogenase, glutamic-oxaloacetic transaminase, and pyruvate kinase were greatly increased in the red cells of children with hemolytic anemia, they were not decreased in the red cells of children with erythroblastopenia of childhood. Only the activity of pyrimidine 5'-nucleotidase was consistently low red cells of these children. These findings are inconsistent with the usual concept that red cell enzyme activities decline throughout red cell life span. Rather, they suggest that there may be very rapid loss in the activity of some red cell enzymes during the first few days of red cell life with little further decline in enzyme activity.
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PMID:Age-related red cell enzymes in children with transient erythroblastopenia of childhood and with hemolytic anemia. 298 25

In early experiments Ah receptor appeared to be localized in cytosol when in its unoccupied state and it was thought that the receptor translocated into nuclei only when occupied by its ligands. However, a recent report [Whitlock and Galeazzi (1984) J. Biol. Chem. 259, 980-985] concluded that unoccupied Ah receptor in the intact cell was primarily located within the nucleus and that apparent 'cytosolic' Ah receptor was a redistribution artifact caused by fractionation of cells in large volumes of buffer. We examined the effect of buffer volume and ionic strength on apparent 'cytosolic' versus 'nuclear' distribution of unoccupied Ah receptor in liver from C57BL/6J mice and Sprague-Dawley rats as well as Hepa-1c1c9 cells in culture. In all three systems the Ah receptor appears to shift out of the nuclear fraction and into the cytosolic fraction as the volume of buffer is increased or when the ionic strength of the buffer is increased. In each system, however, the distribution of the Ah receptor was identical to the distribution of each of three standard cytosolic marker enzymes: aldolase, glucose-6-phosphate dehydrogenase and lactate dehydrogenase. Co-distribution of unoccupied Ah receptor with these cytosolic marker enzymes during fractionation at varied buffer volumes and ionic strengths makes it seem unlikely that the unoccupied receptor is predominantly a 'nuclear' component in intact cells. Marker enzyme data favor an interpretation that unoccupied Ah receptor is primarily cytoplasmic or that this soluble protein is in equilibrium between cytoplasm and nucleus.
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PMID:Ah receptor for 2,3,7,8-tetrachlorodibenzo-p-dioxin. Codistribution of unoccupied receptor with cytosolic marker enzymes during fractionation of mouse liver, rat liver and cultured Hepa-1c1 cells. 300 22

Enzymes of the glycolytic pathway as well as some ancillary enzymes were studied in normal red cells parasitized with Plasmodium falciparum in culture at varying parasitemias as well as in isolated parasites. The levels of all enzymes except diphosphoglycerate mutase, glucose-6-phosphate dehydrogenase, and adenylate kinase were elevated. Extreme elevations of hexokinase, aldolase, enolase, pyruvate kinase, and adenosine deaminase concentrations were noted. In most cases, electrophoretically distinct bands of enzyme activity were also seen. These findings partly explain the previously noted 50- to 100-fold increase in glucose consumption of infected red cells and suggest that further knowledge of these parasite enzymes and their genetic basis may aid both in designing new chemotherapy and in understanding the evolution of these parasites.
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PMID:The enzymes of the glycolytic pathway in erythrocytes infected with Plasmodium falciparum malaria parasites. 305 30

Mutants of mucoid Pseudomonas aeruginosa defective in fructose-bisphosphate aldolase (FBA), NADP-linked glyceraldehyde-3-phosphate dehydrogenase (GAP) or 3-phosphoglycerate kinase (PGK) were unable to grow on gluconeogenic precursors like glutamate, succinate or lactate. The gap and pgk mutants could grow on glucose, gluconate or glycerol, but fba mutants could not. This suggests that the metabolism of glucose or gluconate does not require either PGK or NADP-linked GAP but does require the operation of the aldolase-catalysed step. For gluconeogenesis, however, all three steps are essential. Recombinant plasmids carrying genes for FBA, PGK, GAP or phospho-2-keto-3-deoxygluconate aldolase (EDA) activities were constructed from a genomic library of mucoid P. aeruginosa selecting for complementation of deficiency mutations. Analysis of their complementation profile indicated that one group of plasmids carried fba and pgk genes, while another group carried eda, 6-phosphogluconate dehydratase (edd) and glucose-6-phosphate dehydrogenase (zwf) genes. The gap gene was not linked to any of these markers. Partial restoration of FBA activity in spontaneous revertants of Fba- mutants was accompanied by a concomitant loss of PGK activity. These experiments indicate a linkage between the fba and pgk genes on the P. aeruginosa chromosome.
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PMID:Gluconeogenic mutations in Pseudomonas aeruginosa: genetic linkage between fructose-bisphosphate aldolase and phosphoglycerate kinase. 311 66

Activity of glucose-6-phosphate dehydrogenase (I), fructose diphosphate aldolase (II) and succinate dehydrogenase (III) and content of pyruvate (IV) in the mycelium of the oleandomycin-producing organism were studied during increased intensity of the antibiotic synthesis. The increase in the intensity of the antibiotic synthesis was induced by exposure of the spores to a surface active substance, twin-21. After the exposure a rise in the activity of all the three enzymes in the phase of the culture intensive growth was observed. During the antibiotic intensive production the cultures with increased antibiotic production levels were characterized by significantly higher activity of I as compared to the control while the activity levels of II and III were approximately the same. It was shown that concentration of IV in the mycelium during the antibiotic intensive biosynthesis decreased and the decrease was more pronounced after exposure to twin-21.
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PMID:[Effect of surface-active substances on carbohydrate metabolism in the producer of oleandomycin]. 332 23

Red blood cells (RBCs) from 15 normal human blood samples were incubated with different concentrations of hydrogen peroxide in sodium azide, and the effects of the peroxidation on several glycolytic and nucleotidic enzyme activities were investigated. The release of malonyl dialdehyde (MDA) and methemoglobin formation were used as indicators of RBC peroxidation. The increase of H2O2, final concentration from 0.1 to 5 mmol/l, resulted in a progressive rise of almost all glycolytic enzyme activities, especially those of aldolase (200% of normal at 1 mmol/l), phosphoglycerate kinase (140%), phosphoglycerate mutase (136%), pyruvate kinase (130%) and glutathione peroxidase (130%), and in a decrease of glucose-6-phosphate dehydrogenase (68%) and pyrimidine-5-nucleotidase (23%). The addition of beta-mercaptoethanol to the incubation medium abolished only the effect of 1 mmol/l H2O2 on glucose-6-phosphate dehydrogenase.
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PMID:Increase of enzyme activities following the in vitro peroxidation of normal human red blood cells. 334 32

A procedure for the simultaneous purification to homogeneity of hexokinase, phosphoglucomutase 1 and 2, aldolase, phosphoglucose isomerase and glucose-6-phosphate dehydrogenase from human origin has been developed. Human placenta homogenate was first chromatographed on DE-52 column which retains hexokinase and glucose-6-phosphate dehydrogenase while the other enzymes are recovered in the unabsorbed protein fraction. The other steps in the purification involve Matrex gel and specific affinity chromatography for the DE-52 retained enzymes and phosphocellulose and Matrex gel chromatography for the other enzymes. All the enzymes mentioned were obtained in one week, with recoveries from 14 percent for glucose-6-phosphate dehydrogenase to 75 percent for hexokinase. Thus, the procedures utilized seem to be useful in obtaining large amounts of enzymes in a a homogeneous form from an easily available human tissue.
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PMID:Simultaneous preparation from human placenta of several enzymes of glucose metabolism. 337 5

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

Effect of naphthoquinone levels on the activity of enzymes involved in glycolysis and pentose phosphate cycles was studied in male rats. Under conditions of primary and secondary K-avitaminosis the enzymatic activity, limiting these cycles, (aldolase of fructose-1,6-diphosphate, glucose phosphate isomerase and glucose-6-phosphate dehydrogenase) was increased, while the mitochondrial glutamate dehydrogenase activity was decreased. As a result of metabolic transformations under conditions of K-avitaminosis (primary and secondary) concentration of DNA in the animal tissues was lowered.
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PMID:[The effect of vitamin K on the activity of glycolysis and pentose phosphate cycle enzymes]. 342 Aug 14

The requirement for gluconeogenesis and the pentose phosphate pathway in sporulation of Saccharomyces cerevisiae was investigated using homozygous diploids with mutations in selected portions of the respective metabolic pathways. Mutations affecting the genes FBA1 (fructose-1,6-bisphosphate aldolase), GPM1 (phosphoglycerate mutase) and ZWF1 (glucose-6-phosphate dehydrogenase) were used. Homozygous diploids bearing either fba1-11 or gpm1 mutations were asporogenous, indicating an absolute requirement for gluconeogenesis in sporulation. A strain homozygous for the zwf1 mutation sporulated, but at a reduced level compared to the wild-type. Homozygous spd1-1 mutations restored the ability to sporulate in fba1-11 homozygous diploids; this is believed to occur as a consequence of reduced NH+4 levels in spd1-1-bearing strains, the reduced intracellular NH+4 content serving to promote gluconeogenesis via the residual low levels of enzyme activity present in such mutants.
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PMID:A genetic and biochemical analysis of the role of gluconeogenesis in sporulation of Saccharomyces cerevisiae. 354 Feb 6


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