原牛心脏丙酮酸脱氢酶复合体激酶活性的研究。
An investigation of the kinase activity of aurochs heart pyruvate dehydrogenase complex.
作者信息
Czygier M, Strumilo S
机构信息
Department of Biochemistry, University of Warsaw, Bialystok, Poland.
出版信息
Biochem Mol Biol Int. 1995 Oct;37(2):313-7.
The purified aurochs heart pyruvate dehydrogenase complex (PDC) saturated to approximation 60% with endogenous thiamine pyrophosphate (TPP), was slowly and incompletely inactivated by its kinase in the presence of ATP. Exogenous TPP or ADP, but not pyruvate, strongly inhibited the kinase activity. The kinetic properties of the aurochs heart PDC kinase suggested the occurrence of two active sites each with different affinities for ATP (K'm - 1.7 microM, K''m = 48 microM).
纯化后的原牛心脏丙酮酸脱氢酶复合物（PDC）内源性硫胺素焦磷酸（TPP）饱和度约为60%，在ATP存在的情况下，其激酶可缓慢且不完全地使其失活。外源性TPP或ADP（而非丙酮酸）可强烈抑制激酶活性。原牛心脏PDC激酶的动力学特性表明存在两个活性位点，每个位点对ATP具有不同的亲和力（K'm = 1.7 microM，K''m = 48 microM）。
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