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)

By means of fructose-1,6-diphosphate selective elution of aldolase isoenzymic forms from the phosphocellulose column the izoenzyme AC3 was isolated preparatively from the muscles rabbits with experimental E-avitaminosis muscular dystrophy. The specific activity of aldolase A4 and AC3 with pathology differs from that at normal state by fructose-1,6-diphosphate and fructose-1-monophosphate. As to the electrophoretic activity the isoenzymes A4 and AC3 are similar to the same isoforms at normal state. The values of the Michaelis constants and maximal rate are determined for aldolases A4, AC3 and C4 at normal state and for A4 and AC3 with E-avitaminosis. Differences in these parameters are found relative to two substrates for A4 aldolase and AC3-hybrid at normal state and with dystrophy.
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PMID:[Comparative studies of the properties of aldolase isoenzymes A-C in normal rabbit brain and in skeletal muscles from rabbits with E-avitaminosis dystrophy]. 125 54

A sensitive sandwich-type enzyme immunoassay for the aldolase isozyme, A4, was developed using purified antibodies specific to the A subunit of aldolase. The antibodies were raised in sheep being immunized with purified aldolase A4 and then purified by immunoaffinity chromatography on a column of aldolase A4-coupled Sepharose. The assay system consisted of polystyrene balls with immobilized antibody F(ab')2 fragments and the same antibody F(ab')2 fragments labeled with beta-D-galactosidase from Escherichia coli. The assay was sensitive enough to detect 10 pg/tube of aldolase A4. The assay was specific to the A subunit of aldolase (aldolase A). It cross-reacted about 40% to aldolase A3C, 7% to A2C2 and 0.3% to AC3, but not cross-reacted with C4 nor B4. Coefficients of variation in intra- and inter-assay were less than 16%. Serum aldolase A levels were determined in healthy adults, which were about 200 ng/ml. The distribution and concentrations of immunoreactive aldolase A in various human tissues were also determined. High concentrations of aldolase A were found in skeletal muscle, heart muscle, cerebrum and lymphatic tissue.
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PMID:Sensitive enzyme immunoassay for human aldolase A. 218 23

A sensitive sandwich-type enzyme immunoassay for brain-type isozyme of human aldolase C4 was developed using purified antibodies specific to the C subunit. The antibodies were raised in rabbits by injecting the purified aldolase C4, and purified by means of immunoaffinity chromatography on a column of aldolase C4-coupled Sepharose. The assay system consisted of polystyrene balls with immobilized antibody F(ab')2 fragments and the same antibody Fab' fragments labelled with beta-D-galactosidase from Escherichia coli. The assay was highly sensitive and the minimum detection limit of aldolase C4 was 3 pg/tube. The assay was specific to the C subunit of aldolase (aldolase C). It cross-reacted about 60% with aldolase AC3, 30% with aldolase A2C2, and 4% with aldolase A3C, but showed no cross-reactivity with aldolase A4, the muscle-type isozyme. Coefficients of variation in within-run and between-run precision studies for serum aldolase C were less than or equal to 11%. Serum aldolase C levels in healthy adults of various ages (16-59 yr old) and both sexes ranged from 8.74-18.9 ng/ml. Immunoreactive aldolase C in the extracts of various human tissues was determined. It was distributed at high concentrations in the central nervous tissue and heart and at significant levels in liver, adrenal glands and testis. The assay of aldolase C in cerebrospinal fluid or serum by employing this sensitive immunoassay might be useful in the diagnosis of neurological disorders or acute myocardial damage.
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PMID:Highly sensitive enzyme immunoassay for human brain aldolase C. 351 98

GLycolytic enzymes were studied from normal human retinas (both fetal and adult) and from retinoblastomas of eight patients and an established retinoblastoma cell line. No significant differences were found between the enzyme activities in the tissues investigated except for hexokinase and pyruvate kinase, which were significantly decreased in the tumor cells. In fetal retina, five different forms of pyruvate kinase could be detected by electrophoresis (K4, K3M, K2M2, KM3, and M4). In adult retina the K4 isozyme is almost absent, while in retinoblastoma the M4 isozyme is hardly present. In the retinoblastoma cell line, the M4 isozyme is completely absent. Alanine inhibition of pyruvate kinase from the retinoblastoma cell line is more inhibited compared to the pyruvate kinase of fetal retina and retinoblastoma and is even more inhibited compared to adult retina. Electrophoresis of aldolase from adult retina revealed the presence of all potential A-C hybrids (A4, A3C, A2C2, AC3, and C4). Fetal retina, however, is characterized by the predominance of the A type. The same patterns were observed in the retinoblastoma cell line and retinoblastoma. However, in other brain tumors, e.g., gliomas of adults, a five-membered A-C hybrid set is found. Electrophoresis of hexokinase from normal fetal and adult retina revealed the predominance of hexokinase type I; retinoblastoma and retinoblastoma cell line are both characterized by the presence of considerable amounts of hexokinase type II. The isozyme shifts in retinoblastoma result in an enzyme pattern identical to that of fetal retina except for the presence of hexokinase type II.
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PMID:Characterization of some glycolytic enzymes from human retina and retinoblastoma. 710 15