Moreno S, Paveto C, Passeron S
Acta Physiol Lat Am. 1976;26(5):343-8.
Adenosine 3', 5'-monophosphate (cAMP) dependent protein kinase from yeast cells of Mucor rouxii was partially purified and examined by sedimentation in sucrose density gradients. In the presence of histone and cAMP this procedure allowed the separation of the catalytic moiety from the cAMP binding activity, indicating that the enzyme had dissociated into subunits. The dissociation was accompanied by conversion of the enzyme activity from a cAMP dependent to a cAMP independent form.
来自鲁氏毛霉酵母细胞的3',5'-环磷酸腺苷(cAMP)依赖性蛋白激酶经过部分纯化,并通过在蔗糖密度梯度中沉降进行检测。在组蛋白和cAMP存在的情况下,该方法能够将催化部分与cAMP结合活性分离,表明该酶已解离成亚基。这种解离伴随着酶活性从cAMP依赖性形式转变为cAMP非依赖性形式。