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  • Title: Enhanced phosphorylation of yeast endogenous substrates by phosphatidylglycerol (dioleoyl) and phosphatidylinositol.
    Author: Kuo WN, Ganesan U, Jean MN, Davis DL, Walbey DL, McCall LK, Gurnee ML.
    Journal: Biochem Mol Biol Int; 1994 Mar; 32(4):633-9. PubMed ID: 8038714.
    Abstract:
    Protein kinases and their endogenous substrates from the crude cytosolic extract of Saccharomyces cerevisiae were coeluted in the fraction 13 on DE-52 column chromatography. Analyses of SDS-polyacrylamide gel electrophoresis and autoradiography revealed that the peptides between 14 and 34 kDa were the major phosphorylated substrates. In the presence of Ca2+ and Mg2+, the phosphorylation was suppressed strongly by the regulatory subunit of cAMP-dependent protein kinase and slightly by oleic acid, whereas it was augmented appreciably by phosphatidylglycerol (dioleoyl) and phosphatidylinositol.
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