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)

The author carried out on 35 cats a study on the protein content, potasium and sodium. aldolase, GOT, GPT and LDH of the uterine muscle. The animals were divided into three groups: first-15 nonpregnant cats, second-10 pregnant cats at the first half of pregnancy and third-10 pregnant cats at the second half of pregnancy. He used a piece of uterine muscle from which proteins were extracted by solutions of potasium iodide with various strength. The total protein was determined by the method of Loury, but the sarcoplasmic proteins were examined electrophoretically. Electrolytes were estimated by flame photometer. The enzyme activity was examined by the reagents of "Boehringer". There was an increase of the amount of myosin and of the enzyme active sarcoplasmic protein fraction in the myometrium of pregnant animals. Potasium was increased in the uterine muscle during pregnancy, but sodium decreased. Enxyme activity of ALD, GOT and GPT was the highest in animals from the second group, but that of LDH-in the third group.
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PMID:[Biochemical changes in the myometrium of pregnant cats]. 124 Aug 2

In order to elucidate the effects of amphotericin B (AMB) on the glycolytic pathway, the metabolism of [1-13C]glucose in glucose-grown repressed Saccharomyces cerevisiae was studied. The cells were aerobically suspended in pyrophosphate solutions of high potassium concentration with or without 10(-6) M amphotericin B and measurements were made using 1H-, 13C-NMR spectroscopy and biochemical methods. The results were compared with those obtained under the same experimental conditions but in a medium rich in sodium salts containing the same antibiotic concentration. In general the presence of 10(-6) M AMB reduces the glucose consumption and the ethanol production while favouring the glycerol and trehalose formation. These effects are greatly reduced when a high K+ concentration was used. The AMB effects on the glucose consumption and the production of ethanol, glycerol and trehalose, observed in a suspension rich in Na+, can be fairly well explained by the leakage of K+ through AMB membrane channels. This outflux induces a substantial decrease in the activity of some K(+)-dependent enzymes, such as aldolase, phosphofructokinase and pyruvate kinase. The intensities of the glutamate C2 and C4 signals are higher with a suspension rich in Na+ than with a suspension rich in K+, suggesting that the Krebs cycle operates more effectively in a solution rich in Na+. In the absence of AMB, the passive diffusion of glycerol through the cell membrane is relatively slow and apparently depends on the ionic external medium: it is more efficient in solutions with a high K+ than with a high Na+ concentration. In the presence of 10(-6) M AMB, the glycerol C1,3 resonance drastically decreases at 20 min and then disappears in the noise. This rapid disappearance suggests that glycerol can easily pass through the pores arising from the interaction of AMB with the membrane sterols. However, the rate of pore formation is slow, independent of the external medium (Na+ or K+) and this process is not completed within 20 min.
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PMID:Comparative study of the effects of amphotericin B on the glucose metabolism in Saccharomyces cerevisiae in K(+)- and Na(+)-rich media. 132 8

The frequent association of myotonia with dystrophy and the knowledge that calcium is increased in injured skeletal muscle cells suggest a possible relationship between cell calcium and myotonic alterations. This investigation has been performed to study the role of calcium in experimental myotonia induced by anthracene-9-carboxylic acid (9-AC) in rats treated with several regimens of food and exercise. Thirty-two rats were divided into 4 groups of 8 rats each, one control and 3 experimental groups. The treatments included caffeine plus exercise (group 2), and a calcium-rich diet (group 3); these procedures were designed to increase intracellular calcium; another group was treated with 9-AC as a myotonia-inducer (group 4). The treatment for all groups lasted 60 days. No significant differences in plasma sodium, potassium, chloride and calcium between control and experimental groups were observed. Whole muscle calcium in wet tissue samples did no change with any treatment. On the contrary, mitochondrial calcium showed a significantly higher concentration in group 3 and 4. CPK and aldolase activities in groups 1, 2 and 3 were similar; but in group 4 these enzyme activities were significantly higher (p less than 0.05). The electrical and mechanical responses were not altered in any rat with any experimental treatment. Our data suggest that myotonia is a predisposing factor for an altered mitochondrial calcium homeostasis in this model; in addition, the enzyme activities of CPK and aldolase were increased in the rats of group 4 implicating that myotonia is a crucial factor in the development of enzymatic abnormalities.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Effect of myotonia induced by anthracene-9-carboxylic acid on mitochondrial calcium, plasma creatinine-phosphokinase and aldolase activity in the rat. 139 15

Candida albicans antigens which reacted with immunoglobulin E (IgE) antibodies of 57 allergic patients were detected by immunoblotting. Of the various antigens, the 175-, 125-, 46-, 43-, and 37-kDa antigenic components reacted most frequently with the patient sera. To purify the major antigens, C. albicans cells were fractionated. The 46-, 43-, and 37-kDa antigens were recovered in cytoplasmic fractions, but the 175- and 125-kDa antigens were not recovered in any fraction. The 46-, 43-, and 37-kDa antigens were purified from cytoplasmic fractions by DEAE and P11 ion-exchange chromatography. Antigens were isolated by cutting bands out of sodium dodecyl sulfate-polyacrylamide gels. The purified components confirmed by immunoblotting were next processed for amino acid sequencing. Parts of the sequences of the 46-, 43-, and 37-kDa antigens had significant levels of homology with Saccharomyces cerevisiae glycolytic enzyme enolase, phosphoglycerate kinase, and aldolase, respectively. Rabbit IgG antibodies prepared against the 46- and 43-kDa antigens strongly cross-reacted with the homologous proteins of S. cerevisiae. However, S. cerevisiae enolase and phosphoglycerate kinase did not cross-react with IgE of patient sera. This result suggests that IgE antibodies against only small parts of their epitopes are elevated in the allergic patients. Since enolase is reported to be a major antigen for systemic candidiasis, this enzyme may be the immunodominant protein in both allergies and fungal infections.
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PMID:Identification of Candida albicans antigens reactive with immunoglobulin E antibody of human sera. 154 78

A method for the preparative high-yield electroelution of proteins from sodium dodecyl sulphate (SDS) polyacrylamide gel strips was established. The method consisted of SDS-polyacrylamide gel electrophoresis, detection of proteins with sodium acetate and electrophoretic elution at 200 V for 3 h by utilizing a horizontal flat-bed gel electrophoresis apparatus. Standard proteins with molecular masses of 14-66 kilodalton (cytochrome c, aldolase, ovalbumin and bovine serum albumin) were recovered with an average yield of 73.6 +/- 2.3%. A membrane-bound protein, rat skeletal muscle Ca(2+)-ATPase (100 kilodalton) was also well recovered (over 60%). This method was applicable to the purification of proteins required for N-terminal amino acid sequencing and to raise antibodies.
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PMID:Preparative high-yield electroelution of proteins after separation by sodium dodecyl sulphate-polyacrylamide gel electrophoresis and its application to analysis of amino acid sequences and to raise antibodies. 166 9

Examinations of 176 children administered caries-preventing drugs for 2 years have shown that oral irrigation with 0.2% sodium fluoride solution, oral intake of fluorine in a dose of 1 mg, or of potassium orotate, or of calcium glucerophosphate improved the oral fluid resistance to carbohydrate action. Glycolytic enzyme activity of the oral fluid in these children was not augmenting during carbohydrate load, whereas in children not administered such preventive courses oral intake of 10% glucose solution resulted in essential elevation of salivary aldolase and lactate dehydrogenase activities, i.e. intensification of glycolytic processes, this leading to the development of acid potential in the oral cavity and, consequently, to a higher risk of caries development.
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PMID:[The carbohydrate-resistant mechanism of the action of caries-prophylactic agents on the oral fluid in children]. 179 7

A quantitative histochemical method was developed for the demonstration in rat liver of the activity of phosphofructokinase, one of the enzymes assumed to be rate-limiting for glycolysis. The procedure was based on the reduction of a tetrazolium salt as final electron acceptor and a multistep reaction using the exogenous or endogenous auxiliary enzymes aldolase, triosephosphate isomerase and glyceraldehyde-3-phosphate dehydrogenase. The highest activity was found in unfixed cryostat sections of rat liver when the incubation medium contained 17% (wt/vol) polyvinyl alcohol, 100 mmol/L Tris-maleate buffer (pH 8.4), 20 mmol/L fructose-6-phosphate, 2 mmol/L ATP, 2 mmol/L MgCl2, 5.9 mmol/L NAD+, 0.47 mmol/L 1-methoxyphenazine methosulfate, 5 mmol/L sodium azide and 5 mmol/L Nitro BT. The addition of auxiliary enzymes was not necessary to demonstrate maximum activity in rat liver. The specificity of the reaction was proven by the absence of any specific (test minus control) reaction when the incubation was performed in the presence of 25 mmol/L phosphoenolpyruvate, a competitive inhibitor of phosphofructokinase. Cytophotometric analysis revealed that linear relationships exist between the amount of specific reaction product formed and incubation time and the section thickness. The Km values for fructose-6-phosphate and the Vmax values were not significantly different in periportal and pericentral areas of livers from either normally fed or 24-hr-fasted rats. The homogeneous distribution of phosphofructokinase activity in the liver acinus is in line with biochemical findings using hepatocytes isolated from the two different areas showing that these cells contained similar amounts of enzyme activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Homogeneous distribution of phosphofructokinase in the rat liver acinus: a quantitative histochemical study. 183 3

Ionol, a synthetic antioxidant, limits the stressor liver injury to a greater extent than sodium, valproate and phenazepam, activators of a GABA-ergic link of the stress-limiting organism systems. This injury is exhibited in the organospecific elevated levels of blood enzymes fructosediphosphate aldolase depression of N-demethylase activity of microsomal monooxygenases and a decrease in the amount of cytochromes P-450 and B5.
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PMID:[Comparative evaluation of the protective effect of sodium valproate, phenazepam and ionol in stress-induced liver damage in rats]. 189 54

The presence of low molecular weight GTP-binding proteins was investigated in subcellular fractions from skeletal muscle. Skeletal muscle homogenate, transverse tubules, triads, sarcoplasmic reticulum membranes, and cytosol fractions were separated in sodium dodecyl sulfate-gel electrophoresis and blotted onto nitrocellulose. The presence of GTP-binding proteins was explored by incubation of these blots with [alpha-32P] GTP. GTP labeled two polypeptides of Mr = 23,000 and 29,000 in all the fractions examined. Binding of [alpha-32P]GTP was specific and dependent on Mg2+. The 23-kDa polypeptide was labeled to a higher extent with [alpha-32P]GTP than the 29-kDa polypeptide, although both were enriched in transverse tubule fractions. A GTP-binding polypeptide of 40 kDa was also enriched in transverse tubule preparations and identified as Gi alpha by immunostaining with anti-Gi alpha. Using a blot overlay approach and [alpha-32P]GTP-labeled cytosolic components, several polypeptides were identified that interact with the 23- and 29-kDa GTP-binding proteins. Among these components were polypeptides of Mr = 60,000, 47,000, 44,000, 42,000, and 38,000, which were mainly of cytosolic origin but also associated with triads and transverse tubule membranes. The 47-, 44-, 42-, and 38-kDa polypeptides were found to be structurally related to the glycolytic enzymes enolase, 3-phosphoglyceric phosphokinase, aldolase, and glycoeraldehyde-3-phosphate dehydrogenase, respectively. The purified glycolytic enzymes specifically bound the 23- and 29-kDa GTP-binding proteins under both denaturing and nondenaturing conditions. The association of the GTP-binding proteins with these polypeptides was resistant to detergents such as 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS), Triton X-100, and Tween. A 23-kDa GTP-binding protein purified from chromaffin cells bound to a 157-kDa polypeptide in triads and chromaffin cell membranes. The 157-kDa polypeptide was a minor component in these membranes and not related to the subunits of the dihydropyridine receptor. In view of the proposed function of low molecular weight GTP-binding proteins in processes such as membrane communication and secretion coupling, the association of these proteins with transverse tubules and triads in skeletal muscle is discussed in terms of a role in signal transmission.
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PMID:Identification of low molecular weight GTP-binding proteins and their sites of interaction in subcellular fractions from skeletal muscle. 191 47

Partition equilibrium experiments have been used to characterize the interactions of erythrocyte ghosts with four glycolytic enzymes, namely aldolase, glyceraldehyde-3-phosphate dehydrogenase, phosphofructokinase and lactate dehydrogenase, in 5 mM sodium phosphate buffer (pH 7.4). For each of these tetrameric enzymes a single intrinsic association constant sufficed to describe its interaction with erythrocyte matrix sites, the membrane capacity for the first three enzymes coinciding with the band 3 protein content. For lactate dehydrogenase the erythrocyte membrane capacity was twice as great. The membrane interactions of aldolase and glyceraldehyde-3-phosphate dehydrogenase were mutually inhibitory, as were those involving either of these enzymes and lactate dehydrogenase. Although the binding of phosphofructokinase to erythrocyte membranes was inhibited by aldolase, there was a transient concentration range of aldolase for which its interaction with matrix sites was enhanced by the presence of phosphofructokinase. In the presence of a moderate concentration of bovine serum albumin (15 mg/ml) the binding of aldolase to erythrocyte ghosts was enhanced in accordance with the prediction of thermodynamic nonideality based on excluded volume. At higher concentrations of albumin, however, the measured association constant decreased due to very weak binding of the space-filling protein to either the enzyme or the erythrocyte membrane. The implications of these findings are discussed in relation to the likely subcellular distribution of glycolytic enzymes in the red blood cell.
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PMID:Interactions of glycolytic enzymes with erythrocyte membranes. 214 Feb 76


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