Kinetic properties of cerebral pyruvate kinase
نویسندگان
چکیده
منابع مشابه
Some kinetic properties of liver pyruvate kinase (type L).
Type L pyruvate kinase from mouse liver has been studied. The enzyme is strongly inhibited by low concentrations of copper ions, and the inhibition is reversed by fructose 1,6diphosphate. In the absence of inhibitor, fructose 1,6diphosphate also increases the pyruvate kinase activity at pH values higher than 7. Furthermore, the Cu++ inhibition is pH and K+ concentration dependent. Plots of reac...
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Kinetic properties of rat liver pyruvate kinase type I at pH7.5 and 6.5 were studied with physiological ranges of substrates, modifiers and Mg(2+) concentrations at increasing enzyme concentrations, including the estimated cellular concentrations (approx. 0.1mg/ml). Enzyme properties appear unaffected by increased enzyme concentration if phosphoenolpyruvate, fructose 1,6-diphosphate and inhibit...
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Background: The frequency of pyruvate kinase (PK) deficiency, an autosomal recessive defect, is approximately 3 per 10,000 individuals in Shiraz and surrounding areas, and is increased due to high consanguinity marriage frequency. The purpose of this study is to obtain data on the frequency and spectrum of gene mutation of PK in newborns, from Shiraz and surrounding areas. Materials and Methods...
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Hitherto it has been generally supposed that pyruvate kinase (EC 2.7.1.40) has no significant role in the regulation in vivo of glycolytic flux in skeletal muscle (Carbonell et al., 1973). This supposition, apart from providing an explanation for the apparent lack of potentially regulatory allosteric interactions by skeletal-muscle (M-type) pyruvate kinase, is in agreement with the idea that gl...
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Fast protein liquid chromatography on Superose 6 o f crude extracts from the chlorophyllfree mutant no. 20 o f the unicellular green alga Chlorella kessleri reveals two possibly o ligo meric forms o f pyruvate kinase (2.7.1.40). Their occurrence is markedly altered in the course o f heterotrophic growth with changing levels o f exogenous glucose as carbon source with only one enzyme species wi...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1974
ISSN: 0264-6021
DOI: 10.1042/bj1410165