Eyster K M
Department of Physiology and Pharmacology, University of South Dakota, Vermillion 57069.
Biochem Biophys Res Commun. 1990 Apr 30;168(2):609-15. doi: 10.1016/0006-291x(90)92364-6.
Removal of contaminating proteins from rat ovarian cytosol by DEAE chromatography results in a 358% recovery of protein kinase C activity. The data suggest that rat ovaries contain an endogenous inhibitor of protein kinase C whose activity dominates that of protein kinase C in the cytosol. The inhibitor is specific for protein kinase C and does not activate the enzyme through proteolysis. This endogenous inhibitor may be important in the hormonal control of protein kinase C in the rat ovary, and may become an important tool in the study of the role of protein kinase C in other cell functions.
通过DEAE色谱法从大鼠卵巢胞质溶胶中去除污染蛋白后,蛋白激酶C活性的回收率达358%。数据表明,大鼠卵巢含有一种蛋白激酶C的内源性抑制剂,其活性在胞质溶胶中占主导地位。该抑制剂对蛋白激酶C具有特异性,不会通过蛋白水解激活该酶。这种内源性抑制剂可能在大鼠卵巢蛋白激酶C的激素调控中起重要作用,并且可能成为研究蛋白激酶C在其他细胞功能中作用的重要工具。