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)

NAD-Sepharose 4B gel was used to study the complexation between glyceraldehyde-3-phosphate dehydrogenase (D-glyceraldehyde-3-phosphate:NAD+ oxidoreductase (phosphorylating) EC 1.2.1.12) and aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13). An affinity sorbent specific for glyceraldehyde-3-phosphate dehydrogenase was utilised in a batch system. The dissociation constant of the enzyme complex was calculated. The method elaborated in our laboratory was used to investigate the effects of temperature and pH on the complex formation.
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PMID:Characterization of enzyme-enzyme interaction using an affinity batch system. 710 69

During a long-term study in the rat some enzyme activities were determined in plasma, lung, spleen and skeletal muscle. Twelve rats of each sex were investigated every 49 days from 35 until 1115 days of life. Lactate dehydrogenase in lung and spleen decreases; in muscle and plasma, however, the activity varies considerably. Malate dehydrogenase in the tissues remains nearly unchanged apart from distinct peaks in the first year of life; in plasma the activity takes an M-shaped course. In contrast to the changes of glutamate dehydrogenase in the tissues with a tendency to diminish, this enzyme increases in plasma during the lifetime. Aspartate aminotransferase activity in the tissues, except muscle, varies with a rhythmical behaviour, and in plasma shows a gradual increase. Alanine aminotransferase in lung and spleen has two activity peaks. In muscle this enzyme varies only slightly after a steep initial decrease. In plasma the activity has a tendency to rise. Creatine kinase in the tissues reveals several activity peaks. In plasma the activity course is U-shaped. Adenylate kinase in spleen and lung rises, whereas in muscle the activity varies considerably. The nearly identical decrease of alkaline phosphatase activity in the tissues during ageing is also reflected by a concomitant behaviour in plasma. Leucine arylamidase in lung and muscle both have a U-shaped characteristic, whereas in spleen the activity changes in a shorter period. In plasma, a rhythmical behaviour is apparent. Aldolase in plasma tripled during the observation period. Except for lactate dehydrogenase and aldolase, distinct sex-differences are observed in plasma. With progressive age the animals suffer increasingly from characteristic diseases, which beside experimental components have influenced the enzyme pattern. Enzyme activities in plasma and tissues show a complex pattern and are only of limited importance in understanding the ageing process.
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PMID:Long-term observation of plasma and tissue enzyme activities in the rat. 720 25

Aldolase and pyruvate kinase isozymes were investigated in cultured hepatocytes from fetal, regenerating, and 2-acetyl-aminofluorene-fed rat liver as well as in some epithelial liver cell lines. Our results show that: (a) cell proliferation and prolonged expression of specific isozymes were found only in cultured hepatocytes from 17-day old fetuses; (b) the fetal type of pyruvate kinase expressed in regenerating and carcinogen-treated liver was temporarily lost only in cultured hepatocytes from regenerating liver; (c) the adult type of aldolase and pyruvate kinase was absent in one epithelial cell line derived from a carcinogen-treated liver and in the hepatoma tissue cell (HTC) line but was found in the Faza clone of the Reuber H35 cell line during the 50 first passages in vitro; and (d) the isozyme pattern of pyruvate kinase was always more strongly shifted than that of aldolase. The observations suggest that: (a) hepatocytes from carcinogen-treated liver exhibit the same lack of ability to proliferate in primary culture as normal adult hepatocytes; (b) adult hepatocytes can produce fetal isozymes without prior cell division; (c) pyruvate kinase is a stronger marker of dedifferentiation (retrodifferentiation) than aldolase; and (d) regulatory processes of isozyme expression are different during ontogenesis, regeneration, and hepatocarcinogenesis.
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PMID:Isozyme differentiation of aldolase and pyruvate kinase in fetal, regenerating, preneoplastic, and malignant rat hepatocytes during culture. 725 Sep 94

The intralysosomal localization of the enzymes that catalyse inactivation of rat liver fructose-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) to a form with antigenic activity was demonstrated. The inactivating enzymes like all other lysosomal markers tested except acid phosphatase, were readily solubilized by hypotonic shock. The inactivating enzyme activity was inhibited by PMSF, TPCK, TLCK and leupeptin, but not by pepstatin. On partial purification of the inactivating activity from the lysosomal fraction by DEAE-Sephadex (A-50) and Sephadex G-100 column chromatographies, it was copurified with lysosomal carboxypeptidase A and cathepsin B (EC 3.4.22.1). Studies on its substrate specificity and sensitivity to inhibitors indicated that cathepsin B and carboxypeptidase A are responsible for almost all the aldolase-inactivating activity in the lysosomal fraction.
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PMID:Properties of fructose-1,6-bisphosphate aldolase inactivating enzymes in rat liver lysosomes. 726 Jan

Stress dependent variations in th properties of the rat muscle aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) have been linked to the corresponding changes in the levels of proteolytic activities in rat muscle. Whole-body X-irradiation of rat was shown to result in loss of muscle aldolase activity towards fructose 1,6-bisphosphate by 50% while fructose 1-phosphate activity remained unchanged (Pote, M.S. and Altekar, W. (1980) Ind. J. Biochem, Biophys. 17, 255-262). Incubation of muscle extract of irradiated rat with that from control rat or rabbit muscle aldolase caused similar changes in aldolase activity. The changes are attributed to the action of catheptic enzymes possessing latency characteristics and capable of using aldolase as a substrate; the time course of their increase after irradiation corresponds to that of loss in muscle aldolase activities. Exposure of rats to stress resulted in an increase in the 'free' proteolytic activity, and the concomitant loss of 'bound' activity in muscle lysosomes indicates labilization of lysosomal membrane. The observed degradation of aldolase in vivo by muscle lysosomes is shown to be due to the action of cathepsin B (EC 3.4.22.1) present in the proteolytic enzymes released into cytosol under stress. Inactivation of rabbit muscle aldolase and rat muscle aldolase by rat muscle cathepsin B inhibited by leupeptin, antipain an iodoacetamide, but not be pepstatin. Inactivation is shown to be due to the release of C-terminal tyrosine if aldolase, required for its catalytic activity. Cathepsin B who acts as a rate-limiting enzyme in the degradation of aldolase. Such a proteolytic modification of aldolase in vivo could be relevant not only to the regulation of aldolase activity of glycolysis in muscle but also to the degradation of aldolase during stress conditions related to tissue damage and the maintenance of normal aldolase levels in the blood.
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PMID:Muscle aldolase: the stress-dependent modification of catalytic and structural properties by rat muscle lysosomal cathepsin B. 729 40

The relative concentration of the aldolase x fructose-bisphosphate and of the aldolase x dihydroxy-acetone-phosphate complexes is regulated, in the steady state, by the nature of the accompanying glycolytic enzymes. Particularly in the presence of triose phosphate isomerase, the aldolase x dihydroxyactone-phosphate complexes are largely prevalent. This situation is very likely to hold in rabbit muscle in vivo. Aldolase and gyceraldehyde-3-phosphate dehydrogenase slowly form a complex; however, no evidence has been found for the direct transfer of glyceraldehyde 3-phosphate between the two enzymes.
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PMID:The aldolase-substrate intermediates and their interaction with glyceraldehyde-3-phosphate dehydrogenase in a reconstructed glycolytic system. 739 48

Nervous-system specific aldolase C has been detected in human cerebrospinal fluid (CSF) by radioimmunoassay. Measurement of 138 samples of CSF showed a mean level of 92 +/- 28 ng/ml. There was no correlation between the level of CSF aldolase C and the CSF total protein, albumin, IgG, or IgA levels. Aldolase C immunoreactivity present in concentrated CSF diluted out in parallel with the standard curve in the assay and showed an elution profile on ion-exchange and gel filtration chromatography similar to that of aldolase present in whole human brain extracts. Addition of known quantities of purified aldolase C4 to CSF gave quantitative recovery on subsequent radioimmunoassay. Measurement of aldolase C in the CSF of 66 patients with neurological disorders showed several patients with levels considerably in excess of 120 ng/ml, but there was no statistically significant difference in the mean levels between groups of patients with different diseases.
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PMID:Immunoreactive aldolase C in cerebrospinal fluid of patients with neurological disorders. 740 35

A cytoskeletal fraction of porcine tracheal smooth muscle (PTSM) was found to contain > 90% of total cellular aldolase (fructose 1,6-bisphosphate aldolase, EC 4.1.2.13) activity. PTSM aldolase was purified by DEAE and inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) affinity chromatography and found to react with an antibody directed against human aldolase C, but not anti-aldolase A and B. The molecular mass of native aldolase was about 138 kDa (on Sephacryl S-300); SDS-denatured enzyme was 35 kDa (comigrated with rabbit skeletal muscle aldolase). Total cellular aldolase tetramer (aldolase4) content was 34.5 pmol/100 nmol lipid P(i). Ins(1,4,5)P3) binding activity coeluted with aldolase during Sephacryl 300, DEAE, and Ins(1,4,5)P3 affinity chromatography. Ins(1,4,5)P3 bound to purified aldolase (at 0 degree C) in a dose-dependent manner over the range [Ins(1,4,5)P3] 20 nM to 20 microM, with maximal binding of 1 mol of Ins(1,4,5)P3/mol aldolase4 and a Kd of 12-14 microM. Fru(1,6)P2 and Fru(2,6)P2 displaced bound Ins(1,4,5)P3) with a 50% inhibition at 30 and 170 microM, respectively. Ins(1,3,4)P3 (20 microM) and glyceraldehyde 3-phosphate (2 mM) were also potent inhibitors of Ins(1,4,5)P3 binding, but not inositol 4-phosphate or inositol 1,4-bisphosphate (20 microM each). Aldolase-bound Ins(1,4,5)P3 may play a role in phospholipase C-independent increases in free [Ins(1,4,5)P3].
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PMID:Inositol 1,4,5-trisphosphate binding to porcine tracheal smooth muscle aldolase. 765 22

A procedure has been developed for high-level expression of Trypanosoma brucei fructose-bisphosphate aldolase in Escherichia coli. Therefore, a specific restriction site was introduced by mutagenesis at the front of the gene, enabling its ligation in an expression plasmid, immediately downstream of the regulatory sequences. Growth conditions were established for production of high amounts of soluble and active enzyme. Aldolase was purified to near-homogeneity from the soluble fraction of the bacterial lysate by nuclease treatment, differential precipitation steps, and passage over a CM-Sepharose column. From a 1-liter culture of E. coli cells, 60-120 mg of purified protein that is essentially indistinguishable in physicochemical and kinetic properties and in stability from the enzyme purified from trypanosomes grown in infected laboratory animals was reproducibly obtained.
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PMID:High-level expression of Trypanosoma brucei fructose-1,6-bisphosphate aldolase in Escherichia coli and purification of the enzyme. 775 37

In chickens, as in all vertebrates, tissue-specific expression of aldolase isozymes A, B, and C is developmentally coordinated. These developmental transitions in aldolase expression have been studied most extensively by charting enzyme activity during normal and abnormal development of specific vertebrate tissues. Indeed, aldolase expression has been a key marker for normal differentiation and for retrodifferentiation during carcinogenesis. Aldolase expression during chicken myoblast differentiation offers a model for investigating the regulatory mechanisms of these developmental transitions at the level of gene expression. For these studies, cDNAs encoding the most isozyme-specific regions of both chicken aldolase A and C were cloned. The chicken aldolase A cDNA represents the first report of this sequence. Aldolase steady-state mRNA expression was measured during chicken myoblast differentiation in primary cultures using RNase protection assays with cRNA probes generated from these aldolase cDNA clones. Steady-state mRNA for aldolase C, the predominant embryonic aldolase isozyme in chickens, did not significantly change throughout myoblast differentiation. In contrast, expression of steady-state mRNA for aldolase A, the only aldolase isozyme found in adult-skeletal muscle, was not detected until after myoblast fusion was approximately 50% completed. Aldolase A expression gradually increased throughout myoblast differentiation until approximately 48 h after fusion was completed when there was a dramatic increase. These results are contrasted with those of Turner et al. (1974) [Dev Biol 37:63-89] that showed a coordinated switch in isozyme activities between the embryonic aldolase C and the muscle-specific aldolase A. This discordant expression indicates that the aldolase A and C genes may employ different regulatory mechanisms during myoblast differentiation.
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PMID:Noncoordinate changes in the steady-state mRNA expressed from aldolase A and aldolase C genes during differentiation of chicken myoblasts. 776 78


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