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)

Acute arterial obstruction in hind limb was experimentally induced by intra-arterial injection of sodium laurate saline solution in mongrel dogs, and the inhibitory action of cilostazol (6-[4-(1-cyclohexyl-1H-tetrazol-5-yl)butoxy]- 3,4-dihydro-2(1H)-quinolinone, OPC-13013) on ulcer formation was studied. Cilostazol at oral doses of 10 and 30 mg/kg inhibited ulcer development. Cilostazol inhibited decrease in skin temperature in obstructed hindlimbs in a dose-dependent manner. Cilostazol also inhibited increase of plasma aldolase, creatine phosphokinase and glutamic oxalacetic transaminase activities, presumably due to necrosis of the skeletal muscle.
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PMID:Effect of cilostazol, a new antithrombotic drug, on an experimental model of peripheral circulation insufficiency. 407 28

The reproducibility of the studied biochemical methods was determined by means of the criterion of dispersion of the results approaching the average arithmetic value--the coefficient of variance 'V'. A total of thirty analyses per series were made of one and the same sample, under one and the same conditions, by one and the same laboratory assistant. The blood plasma of cows was studied spectro-photometrically with regard to the levels of urea, total protein, sialic acids inorganic phosphorus, carotene, cholesterin, alkaline phosphatase, aldolase, GOT, GPT, and whole blood (for blood sugar). Complexonometrically, blood plasma was studied for total calcium and magnesium. Flame-photometrically, blood plasma was studied for the content of potassium and sodium; these elements were also followed up in erythrocytes and urine of cows as well as in semen of boars. Employed were methods that were routinely used within the system of the Research and Productional Veterinary Union as suggested by Tsvetkov et al. in their Manual of Methodical Guidance. The values of the coefficient of variance for the variance series of each index were compared to the admissible boundary of V (AB-V) as calculated by Tonks' method. Stated are the sources of mistakes for each of the methods tested, and possibilities are sought to optimize the values of V through eliminating accidental errors.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Reproducibility of spectrophotometric and flame photometric methods]. 409 Feb 65

1. Intracellular concentrations of intermediates and cofactors of glycolysis were measured in guinea-pig cerebral cortex slices incubated under varying conditions. 2. Comparison of mass-action ratios with apparent equilibrium constants for the reactions of glycolysis showed that hexokinase, phosphofructokinase and pyruvate kinase catalyse reactions generally far from equilibrium, whereas phosphoglucose isomerase, aldolase, phosphoglycerate kinase, phosphoglycerate mutase, enolase, adenlyate kinase and creatine phosphokinase are generally close to equilibrium. The possibility that glyceraldehyde 3-phosphate dehydrogenase may catalyse a ;non-equilibrium' reaction is discussed. 3. Correlation of changes in concentrations of substrates for enzymes catalysing ;non-equilibrium' reactions with changes in rates of glycolysis caused by alteration of the conditions of incubation showed that hexokinase, phosphofructokinase, pyruvate kinase and possibly glyceraldehyde 3-phosphate dehydrogenase are subject to metabolic control in cerebral cortex slices. 4. It is suggested that the glycolysis is controlled by two regulatory systems, the hexokinase-phosphofructokinase system and the glyceraldehyde 3-phosphate dehydrogenase-pyruvate kinase system. These are discussed. 5. It is concluded that the rate of glycolysis in guinea-pig cerebral cortex slices is limited either by the rate of glucose entry into the slices or by the hexokinase-phosphofructokinase system. 6. It is concluded that addition of 0.1mm-ouabain to guinea-pig cerebral cortex slices causes inhibition of either glyceraldehyde 3-phosphate dehydrogenase or phosphoglycerate kinase or both, in a manner independent of the known action of ouabain on the sodium- and potassium-activated adenosine triphosphatase.
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PMID:Control of glycolysis in cerebral cortex slices. 422 84

N-Acetylneuraminic acid aldolase from Clostridium perfringens was irreversibly inactivated by 1mm-bromopyruvate with a half-life of 4.2min at pH7.2 and 37 degrees C. The rate of inactivation was diminished in the presence of pyruvate but not with N-acetyl-d-mannosamine, indicating that the inhibitor acted at, or close to, the pyruvate-binding site. The apparent K(i) for bromopyruvate, calculated from the variation of half-life with inhibitor concentration, was 0.46mm, compared with a competitive K(i) 3.0mm for pyruvate. Incubation of the enzyme with radioactive bromopyruvate gave a radioactive, enzymically inactive, protein in which the bromopyruvate had alkylated cysteine residues. Incubation of the enzyme with radioactive pyruvate, followed by reduction with sodium borohydride, led to inactivation of the enzyme and binding of the pyruvate to the protein by reduction of a Schiff's base initially formed with the in-amino group of a lysine residue; only one-twentieth as many pyruvyl residues were bound by this method, showing that bromopyruvate is not specific for the active site. After protection of the enzyme active site with pyruvate, treatment with unlabelled bromopyruvate and dialysis, the enzyme retained 72% activity. When this treated enzyme was separately incubated with radioactive bromopyruvate, or radioactive pyruvate followed by sodium borohydride, the ratio of radioactive pyruvyl residues bound by the two methods was 2.3:1. After reduction and hydrolysis of the bromopyruvate-treated enzyme, the only detectable radioactive amino acid derivative was chromatographically and electrophoretically identical with S-(3-lactic acid)-cysteine. The enzyme was fully active in the presence of EDTA and was not stimulated by bivalent metal ions. It was strongly inhibited by silver and mercuric ions. The apparent molecular weight, determined by Sephadex chromatography, was 250000. A mechanism of action is proposed for the enzyme. Bromopyruvate reacts rapidly at pH6.0 with thiol-containing amino acids. Cysteine appears to react anomalously.
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PMID:Studies on N-acetylneuraminic acid aldolase. 433 37

The chemical synthesis of 4-hydroxy-2-ketopimelic acid is described. An aldolase that cleaves this compound to succinic semialdehyde and pyruvate has been purified from Acinetobacter grown at the expense of 4-hydroxyphenylacetic acid. The molecular weight of the enzyme was about 158,000 from sedimentation equilibrium data; other physical determinations gave values in reasonable agreement. The protein was globular and was dissociated in sodium dodecyl sulfate to give a species of molecular weight 25,700. The enzyme attacked both enantiomers of synthetic 4-hydroxy-2-ketopimelate and was stimulated by Mg(2+) and Mn(2+) ions.
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PMID:Purification and properties of 4-hydroxy-2-ketopimelate aldolase from Acinetobacter. 442 38

Guinea pigs were exposed to sound varying from 2 to 8 kHz in frequency and 80-100 dB (SPL) in intensity for periods of 1 hr. The biochemical parameters, glucose, sodium, total protein, and the glycolytic enzymes, aldolase, phosphohexose isomerase, and total LDH as well as isozymes of the latter were ascertained for blood serum, perilymph, and, in some instances, cerebrospinal fluid. The three enzymes occurred at lower levels in perilymph as compared to blood serum. Except for a small difference in serum total protein, sound presentation incurred no significant effect on any of the above parameters. Definite differences in several metabolites were discerned for perilymph sampled according to scala and which were independent of the respective acoustical treatments. Thus, as compared to the scale tympani, the scala vestibuli perilymph displayed a higher glucose content and a diminished total LDH level and of the latter isozymes, LDH(1) ranged lower and LDH(2), higher. As further evidence pointing to cerebrospinal fluid as the possible origin of perilymph, similarities in glucose contents and LDH isozyme patterns were noted for both fluids.
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PMID:Biochemical parameters of guinea pig perilymph sampled according to scala and following sound presentation. 447 Sep 18

Chromatography of different soluble extracts from HeLa cells on poly(A)-Sepharose columns has allowed the isolation of a protein fraction eluted by 0.2 M NaCl and localized predominantly in the cytoplasmic supernatant and in the 0.5 M KCl ribosomal wash. This fraction is present in large amounts (around 3% of total cytosolic proteins) and appears to contain a major protein species that is acidic on electrofocusing (pI around 4.5) and phosphorylated. It runs on glycerol gradients and Sephadex G-200 chromatography close to the aldolase marker (158,000 daltons) and dissociates into apparently identical subunits of 38,000 +/- 2,000 daltons on sodium dodecyl sulfate-acrylamide gels, suggesting a tetrameric structure.
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PMID:Characterization of a protein species isolated from HeLa cell cytoplasm by affinity chromatography on polyadenylate-sepharose. 452 99

Two reactions in the catabolism of catechol by meta-fission, namely, hydration of 2-oxopent-4-enoate (vinylpyruvate) and aldol fission of the product, are catalyzed by stereospecific enzymes. The absolute configuration of this hydration product was shown to be l(S)-4-hydroxy-2-oxopentanoate. Vinylpyruvate hydratase, purified almost to homogeneity, had a molecular weight of about 287,000 and was dissociated in sodium dodecyl sulfate, without prior treatment with mercaptoethanol, into a species with an approximate molecular weight of 28,000. The hydratase was highly specific for its substrates; thus, although 2-oxo-cis-hex-4-enoate was also hydrated, structurally similar compounds such as the trans isomer, vinylacetic and crotonic acids, and the ring-fission products of catechol and methylcatechols were not attacked. Vinylpyruvate hydratase was activated by Mn(2+) ions. On the basis of these observations, a mechanism is proposed which closely resembles that for 4-hydroxy-2-oxopentanoate aldolase. A possible evolutionary connection between functionally related, divalent cation-activated hydro-lyases and aldolases is discussed. It was also demonstrated that l-(S)-4-hydroxy-2-oxohexanoate is the biologically active enantiomer of this hydroxy acid.
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PMID:Stereospecific enzymes in the degradation of aromatic compounds by pseudomonas putida. 469 Sep 69

Amidination of aldolase, glyceraldehyde-3-phosphate dehydrogenase, tryptophan synthetase B protein, L-arabinose isomerase, and the catalytic subunit of E. coli aspartate transcarbamylase with the bifunctional reagent dimethyl suberimidate produces cross-linked proteins, with reaction predominating within oligomers. Disc electrophoresis of a modified protein on polyacrylamide gel in the presence of sodium dodecyl sulfate resolves a set of species with molecular weights equal to integral multiples of the protomer molecular weight. For oligomers composed of identical protomers, the number of principal species observed is identical to the number of protomers in the oligomer. Application of the method to two proteins composed of dissimilar protomers, native aspartate transcarbamylase and tryptophan synthetase alpha(2)beta(2) complex of E. coli, revealed differences in the reactivities of the different kinds of protomer within each oligomer.
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PMID:Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oligomeric proteins. 491 6

The present work describes procedures in which seven major muscle enzymes and serum albumin can be simultaneously isolated from chicken skeletal muscles. The seven enzymes isolated were: phosphorylase, enolase, creatine-P kinase, aldolase, glyceraldehyde-3-P dehydrogenase, phosphoglycerate mutase, and triose-P isomerase. The proteins isolated by these methods were judged to be greater than 97% pure on the basis of electrophoretic analysis in sodium dodecyl sulfate polyacrylamide gels. The procedure is applicable for isolation of the enzymes from large (greater than 100 g) or small (less than 0.5 g) amounts of muscle tissue and the entire procedure can be completed within two days. Particularly useful features of the procedures are: (1) preferential solubilization of the enzymes from myofibrils by extraction of muscle specimens in solutions of different ionic strength; (2) specific precipitation of phosphorylase, creatine-P kinase, and glyceraldehyde 3-Phosphate dehydrogenase from solutions of specified pH and degrees of ammonium sulfate saturation; and (3) an alternate method for isolation of glyceraldehyde-3-P dehydrogenase by specific elution of the enzyme from phosphocellulose columns with ATP. Because of the ease, rapidity, and reproducibility of the procedures, these methods may be useful for the routine isolation of the muscle enzymes in studies on biochemical regulation, as well as for obtaining large quantitites of the enzymes for structural analysis.
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PMID:A simple procedure for the isolation of seven abundant muscle enzymes. 626 Dec 32


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