Kiss Z, Mhina V
FEBS Lett. 1982 Nov 1;148(1):131-4. doi: 10.1016/0014-5793(82)81258-1.
The treatment of rat liver plasma membranes with EDTA resulted in substantial release of a protein kinase activity. Using histones as external substrates both phosphatidylserine (PS) and diolein activated the enzyme. The activatory effect of PS but not that of diolein depended on Ca2+. In contrast, the enzyme activity was inhibited by both PS and diolein when the substrate was protamine. The inhibition by PS, unlike by diolein, depended on Ca2+. Data suggest that mobilization of plasma membrane-bound Ca2+ by physiological stimuli may be accompanied by release of the lipid-dependent protein kinase into the cytoplasm.
用乙二胺四乙酸（EDTA）处理大鼠肝细胞膜，导致一种蛋白激酶活性大量释放。以组蛋白作为外部底物时，磷脂酰丝氨酸（PS）和二油精均能激活该酶。PS的激活作用依赖于Ca2+，而二油精的激活作用则不依赖Ca2+。相反，当底物为鱼精蛋白时，PS和二油精均抑制该酶活性。与二油精不同，PS的抑制作用依赖于Ca2+。数据表明，生理刺激引起的细胞膜结合Ca2+的动员可能伴随着脂质依赖性蛋白激酶释放到细胞质中。
