Phosphorylation of p36 in vitro with pp60src. Regulation by Ca2+ and phospholipid.
作者： John R. Glenney
DOI: 10.1016/0014-5793(85)80047-8
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摘要: P36 is a major substrate of the tyrosine protein kinases. isolated from bovine intestine was used in phosphorylation reactions with pp60src. Phosphorylation stimulated 3-5-fold by Ca2+, however Km same (2.5 microM) at high or low Ca2+. Although level free Ca2+ needed for this enhanced 10(-4)-10(-3) M, phosphatidylserine shifted sensitivity to 10(-6)-10(-5) M range. Independent evidence suggested that p36 interacts directly liposomes containing phosphatidylserine. This raises possibility p36, like c-kinase, Ca2+-activated, phospholipid-dependent protein.
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