Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: 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)

Fructose diphosphate aldolase (D-fructose-1,6-biphosphate D-glyceraldehyde-3-phosphate lyase, EC 4.1.2.13) from rabbit heart has been purified and obtained in crystalline form. The preparations are homogeneous on the basis of disc gel electrophoresis and ultracentrifugation. The catalytic and the molecular properties indicate that this is aldolase A. A comparison was made between rabbit heart aldolase and the rabbit muscle enzyme. The sedimentation coefficient, energy of activation and Michaelis constant for Fru-1,6-P2 were found to be identical with the values obtained for the muscle enzyme. As in case of the muscle enzyme, heart aldolase was found to have a broad pH optimum, remarkable stability over a wide pH range, and the ability to form a Schiff base intermediate with dihydroxyacetone phosphate upon reduction with borohydride. Cleavage of the methionyl bonds with CNBr yields the same pattern as obtained with the muscle enzyme.
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PMID:Purification and properties of rabbit heart muscle aldolase. 1 26

Hepatocytes from adult rats were maintained in primary culture for up to 10-13 days on nylon meshes coated with a thin layer of rat tail collagen gel. Their ultrastructure closely resembled that of the liver parenchymal cell in vivo, but hepatocytes in late culture exhibited a pronounced buildup of microfilaments beneath their apical cell surface. Hepatocytes in early and late cultures secreted albumin, transferrin, and alpha1-acid glycoprotein into the medium; they exhibited a 7- to 10-fold induction of tyrosine aminotransferase activity by dexamethasone; and they expressed an alkaline phosphatase that was similar to that of normal rat liver with respect to its inhibition by the liver enzyme inhibitor L-homoarginine. In addition, the hepatocytes in culture demonstrated phenotypic changes characteristic of fetal liver parenchymal cells. These changes, which paralleled an increase in DNA synthesis, included the expression of and linear increase in the activity of the fetal liver cell enzyme gamma-glutamyl transpeptidase, an increased production of alpha1-fetoprotein, and a change in the substrate specificity of fructose-bisphosphate aldolase to that of the fetal liver isozyme.
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PMID:Fetal phenotypic expression by adult rat hepatocytes on collagen gel/nylon meshes. 8 1

1) The activities of 16 enzymes of glycolysis and of glutathione metabolism were determined in intact human red cell membranes (ghosts) which were prepared by hypotonic hemolysis. 2) Enzymes and hemoglobin of the ghosts were resolved by two toluene extractions. Only the four enzymes hexokinase, fructose-bisphosphate aldolase, glyceraldehyde-phosphate dehydrogenase and pyruvate kinase could not be released completely from the ghosts. 3) The residual membrane fraction, which was obtained after the toluene extraction of ghosts prepared at 30 imOsM, contained 0.02% of the original hemoglobin content of the red cell. Between 6.5 and 23% of the hemolysate activities of glyceraldehyde-phosphate dehydrogenase, phosphoglycerate kinase, pyruvate kinase and fructose-bisphosphate aldolase were detected in this fraction after mechanical disruption. 4) Sonication of intact ghosts increased the activities of fructose-bisphosphate aldolase, pyruvate kinase and phosphoglycerate kinase. 5) In "white" ghosts prepared at 5 imOsM phosphate buffer which contained 0.5% of the original hemoglobin the activities of fructose-bisphosphate aldolase and glyceraldehyde-phosphate dehydrogenase were detected at high levels. The activities of pyruvate kinase and phosphoglycerate kinase were low in these preparations. 6) The results indicate that one part of all enzymes is loosely attached to the inner surface of the membrane as is hemoglobin. A second part, the "cryptic enzyme activity", is available after resolving by toluene. A residual part of four enzymes is firmly bound to the membrane. Two of them (fructose-bisphosphate aldolase and glyceraldehyde-phosphate dehydrogenase) are oriented toward the inner surface of the membrane, whereas pyruvate kinase and phosphoglycerate kinase are hidden in the lipid core of the membrane.
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PMID:Organization of enzymes of glycolysis and of glutathione metabolism in human red cell membranes. 16 42

The isoenzymatic pattern of aldolase was determined by immunoprecipitation with specific anti-aldolase A, B and C sera in 21 pathological liver tissues and in the sera of normals (n equals 20), liver cirrhotics (n equals 52) and hepatoma patients (n equals 22). The increase of aldolase A in primary liver cell carcinoma is not reflected in the sera of these patients, cannot be used for diagnostic purposes and is not hepatoma-specific.
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PMID:Aldolase isoenzymes in liver cirrhosis and primary liver cell cancer. 16 80

The concept of tumor markers was reviewed, and the potential uses of markers of central nervous system (CNS) tumors and methods for their evaluation were discussed. Markers examined included lactate dehydrogenase, aspartate aminotransferase, fructose-bisphosphate aldolase, the polyamines, desmosterol, and several other enzymatic, nonenzymatic, and immunologic markers. Data collated from the clinical studies surveyed showed isocitrate dehydrogenase, desmosterol, and the polyamines to have the greatest potential utility in the diagnosis of CNS tumors.
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PMID:Biochemical markers of central nervous system tumors measured in cerebrospinal fluid and their potential use in diagnosis and patient management: a review. 38 10

Content of aldolase isoenzymes was reinvestigated in human and rat tissues by means of agar and starch gel electrophoresis. Heterogeneity of the A type aldolase is established and possible causes of formation of the multiple forms of the enzyme are discussed. The ratio of various fractions of aldolase A was different in erythrocytes of newborn and aldult persons. The patterns of the aldolase isozyme spectra were characterized in blood sera of newborns, in acute hepatitis and myocardial infarction.
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PMID:[Characteristics of the molecular diversities of human and rat aldolase via starch and agar gel electrophoresis]. 51 34

The messenger activity for fructose 1,6-bisphosphate aldolase (EC4.1.2.13) (aldolase) A isozyme has been characterized in the polysome- or the messenger RNA-directed, protein-synthesizing system using the pH 5 fraction of rat liver or wheat germ extracts, respectively. The subunit of aldolase A synthesized in vitro was detected by immunoprecipitation with anti-aldolase A antibody raised in chickens followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The synthesis of the enzyme depended on the addition of polysomes or polyadenylate-containing RNA of rat ascites hepatoma AH 7974 cells which show a complete shift of aldolase isozyme to type A, whereas polysomes of adult rat liver were inactive. The messenger activity for aldolase A was present exclusively on free polysomes but absent on membrane-bound polysomes and in the soluble supernatant fraction of AH 7974 cells. The size of aldolase A messenger RNA determined by formamide-containing sucrose density gradient centrifugation was approximately 5.8 X 10(5) daltons corresponding to 1650 nucleotides. Taking into account the number of amino acid residues in the aldolase A subunit, approximately 400 nucleotides correspond to the noncoding region of aldolase A messenger RNA.
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PMID:Characterization of messenger RNA for fructose 1,6-bisphosphate aldolase A isozyme of rat ascites hepatoma AH 7974 cells. 76 Dec 23

The quantitative and qualitative changes in fructose-P2 aldolase isoenzyme concentrations during development of "red" (leg) and "white" (breast) skeletal muscles of the chick were investigated. (a) The aldolase C to A subunit transition associated with muscle development is accompanied by large increases in aldolase activity (units/g, wet weight) and in specific catalytic activity (units/mg of protein). The accumulations in both muscle types follow pseudo-first order kinetics with doubling times of 2 to 3 days. The steady state level of aldolase activity in breast muscle (about 150 units/g) is approximately 4-fold higher than that in leg muscle (about 40 units/g). In contrast to leg muscle, the major increase in aldolase activity in breast muscle occurs during postembryonic development. (b) Immunotitration studies demonstrated a direct correlation between increases in enzyme activity and aldolase A subunits during postembryonic muscle development. It was calculated that under steady state conditions, aldolase A4 comprises about 1 percent and 0.26 percent, respectively, of the total wet weight of breast and leg muscle. (c) regulation at the level of protein synthesis in effecting the postembryonic accumulation of aldolase A4 in the muscle types was investigated in short term amino acid incorporation experiments. After a 1-hour pulse with [3H]leucine, aldolase from breast and leg muscle was isolated in a single step by affinity chromatography on phosphocellulose. Incorporation of tritum into aldolase A4 and into soluble or total protein was compared. Between 4 and 38 days after hatching, the rate of aldolase synthesis relative to the synthesis of soluble muscle protein increased about 7- and 3-fold, respectively, in breast and leg muscle. Relative to total protein, incorporation of [3H]leucine into A4 increased about 3-fold in breast muscle, and decreased slightly in leg muscle between 5 and 25 days after hatching. By 3 weeks after hatching, incorporation of [3H]leucine into aldolase A4 relative to incorporation into total protein was about 6-fold higher in breast muscle than it was in leg muscle. The present work, as well as other recent studies, are discussed in relation to the mechanism involved in controlling tissue-specific and stage-specific levels of aldolase isoenzymes in animal cells.
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PMID:Ontogeny and regulation of fructose diphosphate aldolase isoenzymes in "red" and "white" skeletal muscles of the chick. 80 78

Aldolases A, B and C were determined by immunotitration analysis in extracts of human kidney and small intestine and demonstrated immunohistochemically in tissue sections of the same organs at various stages of development. By both techniques a change of isoenzyme pattern during development of the kidney and the small intestine was observed, leading from the predominance of A-type towards the predominance of B-type aldolase. In the extracts of kidney and small intestine the specific activity of aldolase B--but not that of aldolase A--rises with age by about one order of magnitude. The histochemical investigation showed that the developmental change in aldolase pattern in the organ extracts is caused by the differentiation of proximal tubulus cells in the kidney and the differentiation of epithelial cells in the small intestine. Within these cells an increase in the concentration of aldolase B and a decrease in that of aldolase A takes place during development. The possible physiological role of this cellular change in aldolase isoenzyme pattern is discussed. Aldolase C was found only in low concentrations in fetal organs. Only in the kidney, a specific localization within the proximal tubules could be demonstrated.
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PMID:The changes in aldolase isoenzyme pattern during development of the human kidney and small intestine--demonstrated in organ extracts and tissue sections. 84 1

In human striated muscle obtained in surgery, an age-dependent decrease in aldolase and creatine kinase specific activities and an increase in DNA content per wet weight was found. In the group of the elderly (64-84 years), the enzymes decreased by 40-60% when compared with a group between 24 and 47 years old, while DNA content rose by a factor of 1.53 indicating loss of tissue water. Titration of aldolase and creatine kinase molecules by specific antibodies against aldolase A and creatine kinase MM isozymes, respectively, revealed very little accumulation of aldolase cross-reacting materials in the old age group (1.13 fold), and no accumulation of inactive creatine kinase molecules. Similar conclusions can be drawn from thermostability analyses of these two enzymes. The data do not support the view that accumulation of modified proteins due to random errors or to post-translational alternations is a general or causative phenomenon of aging in human muscle tissue.
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PMID:The age-dependent decrease in creatine kinase and aldolase activities in human striated muscle is not caused by an accumulation of faulty proteins. 99 63


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