Coenzyme-Dependent Conformational Properties of Rat Liver Ornithine Aminotransferase
نویسندگان
چکیده
منابع مشابه
Chemical, physical, and morphological properties of ornithine Aminotransferase from rat liver.
Ornithine aminotransferase was crystallized from rat liver and several properties of the enzyme were studied, including amino acid composition, thiol content, absorbance spectrum, isoelectric point, molecular weight, and appearance under the electron microscope. The half-cystine and thiol contents of the enzyme were equal (0.12 pmole per mg of enzyme), indicating the absence of disulfide bonds ...
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Tyrosine aminotransferase (EC 2.6.1.5) of human liver was purified 2200-fold by successive chromatography on DEAE-cellulose DE-52, Ultrogel AcA-34, CM-Sephadex C-50 and hydroxyapatite to a specific activity of 64 units/mg of protein. The purified enzyme had a molecular mass of 95 500. The Km-values were 1.04 X 10(-3) mol/l, 0.17 X 10(-3) mol/l and 0.69 X 10(-6) mol/l for tyrosine, 2-oxoglutarat...
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Pyruvate, oxaloacetate, and P-ketoglutarate were reported to be inactive (4). In contrast, preparations from rat liver were found to be most active with pyruvate, but oc-ketoglutarate, glyoxylate, and a number of other oc-keto acids also were reactive at appreciable rates (5, 6). The equilibrium for Reaction 1 was shown to be very far towards the right, presumably because of spontaneous convers...
متن کاملStudies on the development of ornithine-keto acid aminotransferase activity in rat liver.
1. During the normal development of the rat, the specific activity of liver ornithine-keto acid aminotransferase exhibits a transient elevation around term, and subsequently increases to adult activity levels during the third postnatal week. 2. The synthetic glucocorticoid triamcinolone, administered as a single injection, produces a marked elevation of the ornithine-keto acid aminotransferase ...
متن کاملImmunochemical Studies of Serine Dehydratase and Ornithine Aminotransferase Regulation in Rat Liver in Viva*
Previous studies of serine dehydratase (EC 4.2.1.13) and ornithine aminotransferase (EC 2.6.1.13) adaptation in rat liver showed that in rats on a high protein diet, glucocorticoid administration increased serine dehydratase activity while simultaneously reducing the activity of ornithine aminotransferase. The present study examines the role of enzyme synthesis in the expression of these and ot...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1976
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1976.tb10935.x