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 activities of hexokinase, phosphofructokinase, aldolase, enolase and pyruvate kinase were studied in breast cancer metastases occurring at various sites and compared with the enzyme activities in a series of primary breast cancers. The activities of all enzymes studied were significantly higher in the metastases compared to the primary tumors (p less than or equal to 0.05). However, no changes in the isoenzyme patterns of enolase and pyruvate kinase were observed when the metastases were compared with primary breast cancers. Differences in location of the metastases did not lead to differences in enzyme activities. Our data suggest an association of an increasing rate of glycolysis with tumor progression.
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PMID:Glycolytic enzyme activities in breast cancer metastases. 297 47

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

Since the discovery of glucose 6-phosphate dehydrogenase (G6PD) and of pyruvate kinase deficiencies, erythroenzymopathies associated with hereditary hemolytic anemia have been extensively investigated. Kinetic and electrophoretic studies have shown that most, if not all, erythroenzymopathies are caused by the production of a mutant enzyme. Except for a few enzymes that are abundant in blood and tissues, it is difficult to obtain enough sample to study the functional and structural abnormalities of mutant enzymes associated with genetic disorders in man. The primary structures of only two normal red cell enzymes which can cause hereditary hemolytic anemia, phosphoglycerate kinase (PGK) and adenylate kinase, have been determined. Single amino acid substitutions of PGK variants have been found, and the identification of the exact molecular abnormalities of such variants has helped us to understand the accompanying functional abnormality. Gene cloning makes possible the identification of the DNA sequence that codes for enzyme proteins. Recently, human complementary DNA (cDNA) for aldolase, PGK, G6PD, and adenosine deaminase (ADA) have been isolated, and the nucleotide sequences for PGK and ADA determined. In the near future, human cDNA sequencing should permit identification of the gene alteration that gives rise to the mutant enzymes.
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PMID:Molecular aspects of erythroenzymopathies associated with hereditary hemolytic anemia. 299 Feb 2

The specific activities of glucosephosphate isomerase, aldolase, triosephosphate isomerase, glyceraldehydephosphate dehydrogenase, phosphoglycerate kinase, phosphoglycerate mutase, pyruvate kinase and lactate dehydrogenase were all higher in the synaptoplasmic fraction from rat brain than in 100,000 g supernatant fraction of rat brain homogenates when the supernatants were prepared in high ionic strength solutions. Four enzymes in synaptosomes and two enzymes in homogenates were associated with particulate fractions as indicated by the large increase in specific activity of the enzymes when samples were treated with 0.3 M KCl before centrifugation. Glucosephosphate isomerase, aldolase, pyruvate kinase and lactate dehydrogenase were the enzymes that showed a large increase in specific activity following salt treatment of isolated, synaptosomal membrane while aldolase and pyruvate kinase were the two enzymes which showed a large increase in specific activity in the high speed supernatant fractions. Because the specific activities of many enzymes are found to be elevated not only in synaptosomes but in synaptosomal membrane fractions it is suggested that these enzymes may provide the potential for significantly enhanced glycolysis at these locations.
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PMID:Glycolytic enzyme levels in synaptosomes. 299 Aug 10

Sarcoplasmic reticulum Ca2+-ATPase, acylphosphatase and other soluble enzymes (creatine kinase, lactate dehydrogenase, aldolase and pyruvate kinase) were assayed in muscle biopsies from patients affected by Duchenne muscular dystrophy (DMD) and from normal controls. Specific activities of all the soluble enzymes were decreased in dystrophic muscle, acylphosphatase exhibiting the most marked and significant decrease comparable to that of creatine kinase, in spite of a moderate increase in serum levels. Also, Ca2+-ATPase, particularly the calcium-dependent activity, was decreased in dystrophic muscle. A positive correlation, higher than with the other soluble enzymes, was obtained between acylphosphatase specific activity and the percentage of Ca2+-activation of Ca2+-ATPase. These findings: suggest an impairment of microsomal calcium uptake which could be, at least in part, responsible for sarcoplasmic calcium accumulation observed in DMD; do not disagree with an hypothesized role of acylphosphatase in intracellular calcium homeostasis, consistent with the enzyme's demonstrated hydrolytic activity on the phosphorylated intermediate of Ca2+-ATPase.
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PMID:Sarcoplasmic reticulum Ca2+-ATPase and acylphosphatase activities in muscle biopsies from patients with Duchenne muscular dystrophy. 302 59

We developed a novel procedure for isolation of the muscle isozymes of aldolase, triose phosphate isomerase (TPI), glyceraldehyde phosphate dehydrogenase (GAPDH), phosphoglycerate kinase (PGK), phosphoglycerate mutase (PGM), enolase, pyruvate kinase (PK) and lactic dehydrogenase (LDH), and also creatine kinase (CK), at high purity, specific activity and yield. Protein was extracted from chicken breast muscle and glycolytic enzymes were purified by a three step procedure consisting of: Ammonium sulfate combined with pH fractionation. Phosphocellulose chromatography with performance of high pressure liquid chromatography, exploiting a pH gradient formed by a gradient of the buffering ion for protein elution. Affinity chromatography causing elution by substrate or pH. The enzymes, obtained at over 95% purity as judged by specific activity and silver stained electropherograms, were injected into sheep. Antibody for each enzyme was purified on specific immunosorbant and its specificity was verified by immunotransfer analysis.
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PMID:High performance purification of glycolytic enzymes and creatine kinase from chicken breast muscle and preparation of their specific immunological probes. 303 10

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

Vesiculated fragments of chicken skeletal muscle transverse tubule (TT) membranes were analyzed for their content of loosely associated and integral membrane proteins. Of particular interest was the identification of the magnesium-stimulated ATPase (Mg-ATPase), which is characteristically located in native isolated TT vesicles of chicken skeletal muscle [R. A. Sabbadini and V. R. Okamoto (1983) Arch. Biochem. Biophys. 223, 107-119]. A number of the proteins found in vesicular TT preparations were found to be extractable by a mild Triton-X100 treatment and were identified as aldolase, enolase, creatine kinase, glyceraldehyde-3-phosphate dehydrogenase, lactate dehydrogenase, and pyruvate kinase. Approximately 60% of TT-associated protein was extracted with Triton, resulting in a twofold enrichment of the Mg-ATPase. Concommitantly, one core integral membrane protein possessing a Mr of 102,000 was enriched, suggesting that it is responsible for the Mg-ATPase activity present in chicken skeletal muscle TT membranes.
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PMID:Characterization of transverse tubule membrane proteins: tentative identification of the Mg-ATPase. 315 29

Interactions of glucose-6-phosphate isomerase (D-glucose-6-phosphate ketol-isomerase, EC 5.3.1.9), aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13), glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating), EC 1.2.1.12), triose-phosphate isomerase (D-glyceraldehyde-3-phosphate ketol-isomerase, EC 5.3.1.1), phosphoglycerate mutase (D-phosphoglycerate 2,3-phosphomutase, EC 5.4.2.1), phosphoglycerate kinase (ATP:3-phospho-D-glycerate 1-phosphotransferase, EC 2.7.3), enolase (2-phospho-D-glycerate hydro-lyase, EC 4.2.1.11), pyruvate kinase (ATP:Pyruvate O2-phosphotransferase, EC 2.7.1.40) and lactate dehydrogenase [S)-lactate:NAD+ oxidoreductase, EC 1.1.1.27) with F-actin, among the glycolytic enzymes listed above, and with phosphofructokinase (ATP:D-fructose-6-phosphate 1-phosphotransferase, EC 2.7.1.11) were studied in the presence of poly(ethylene glycol). Both purified rabbit muscle enzymes and rabbit muscle myogen, a high-speed supernatant fraction containing the glycolytic enzymes, were used to study enzyme-F-actin interactions. Following ultracentrifugation, F-actin and poly(ethylene glycol) tended to increase and KCl to decrease the pelleting of enzymes. In general, the greater part of the pelleting occurred in the presence of both F-actin and poly(ethylene glycol) and the absence of KCl. Enzymes that pelleted more in myogen preparations than as individual purified enzymes in the presence of poly(ethylene glycol) and the absence of F-actin were tested for specific enzyme-enzyme associations, several of which were observed. Such interactions support the view that the internal cell structure is composed of proteins that interact with one another to form the microtrabecular lattice.
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PMID:Heteromerous interactions among glycolytic enzymes and of glycolytic enzymes with F-actin: effects of poly(ethylene glycol). 333 56

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


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