Phosphorylation of endogenous substrates of yeast protein kinase C regulated by lipid-triton micelles.
作者信息
Kuo W N, Davis D L, Jean M N, McCall L K, Jones D L, Jn-Baptiste J
机构信息
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32114.
出版信息
Biochem Mol Biol Int. 1994 Oct;34(3):553-9.
PMID:7833832
Abstract
In the DE-52 fraction 19 of the crude cytosolic extract of Saccharomyces cerevisiae, the 31-kDa endogenous substrate(s) of protein kinase C were detected by SDS-polyacrylamide gel electrophoresis and autoradiography. Phosphorylation of the substrate(s) depended on Ca2+, phosphatidylserine and diacylglycerol. It was also enhanced by phosphatidylinositol, phosphatidylethanolamine and phosphatidylglycerol (dioleoyl), but inhibited by arachidonic acid and sphingosine.
摘要
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