Induction of Tyrosine-a-ketoglutarate Transamimase in Rat Liver
نویسنده
چکیده
Previous papers of this series have demonstrated that induction of tyrosine oc-ketoglutarate transaminase of rat liver can be attributed to adrenocortical hormone (1) and described extensive purification of the transaminase from normal and induced livers (2). The present report describes experiments in which the induction phenomenon was analyzed with a highly specific antiserum prepared against the enzyme purified from induced livers. Analysis was directed toward determining whether the increase in activity observed on induction reflects a hormonal stimulation of specific enzyme synthesis or some other mechanism. In a preliminary report (3), the results of precipitin and labeling cxperiments were interpreted as suggesting the existence of an inactive precursor to the enzyme in the noninduced state. The present esperiments, in which a more specific antiserum and techniques for ensuring specificity in immunological assays have been used, confirm the preliminary observations reported, insofar as they demonstrate that enzyme labeling is independent of induction. However, the data also demonstrate that a simple precursorenzyme interconversion is not involved.
منابع مشابه
The Cofactor-mediated Regulation of Apoenzyme Levels in Animal Tissues. I. the Pyridoxine-induced Rise of Rat Liver Tyrosine Transaminase Level in Vivo.
It has so far not been possible to evaluate fully the extent to which the synthesis of apoensymes, in animal organs, may be regulated by cellular concentrations of the substrate or cofactor moiety of the same enzyme system. A few examples of decreased apoenzyme levels have been reported to occur in tissues of animals maintained for some weeks on a diet deficient in the appropriate vitamin or su...
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متن کاملThe effect of hydrocortisone on tyrosine-alpha-ketoglutarate transaminase and tryptophan pyrrolase activities in the isolated, perfused rat liver.
Administration of hydrocortisone or cortisone to rats has been shown to produce a marked increase in hepatic tryptophan pyrrolase (1, 2) and tyrosine-cY-ketoglutarate transaminase’ (4, 5) activities. Although present evidence suggests that the rise in tryptophan pyrrolase activity involves the synthesis of new protein (6) and the rise in tyrosine transaminase activity may not (7), the mechanism...
متن کاملThe Cofactor-mediated Regulation of Apoenzyme Levels in Animal Tissues I. THE PYRIDOXINE-INDUCED RISE OF RAT LIVER TYROSINE TRANSAMINASE LEVEL IN VIVO* OLGA GREENGARD AND MARIA GORDON
It has so far not been possible to evaluate fully the extent to which the synthesis of apoensymes, in animal organs, may be regulated by cellular concentrations of the substrate or cofactor moiety of the same enzyme system. A few examples of decreased apoenzyme levels have been reported to occur in tissues of animals maintained for some weeks on a diet deficient in the appropriate vitamin or su...
متن کاملMetabolic Adaptations in Rat Hepatomas II. Tryptophan Pyrrolase and Tyrosine -Ketoglutarate Transaminase*
The administration of t ryptophan or cortisone to rats bearing the Morris 5123 Hepatoma resulted in significant increases in t ryptophan pyrrolase activity in the host liver but in no change in the low tryptophan pyrrolase activity of the neoplasm. The repressed level of this enzyme in the neoplasm was not a result of the lack or excess of cofactors or enzymes necessary for the assay procedure ...
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تاریخ انتشار 2003