ENZYMATIC CHARACTERISTICS OF PP60V-SRC ISOLATED FROM VANADIUM-TREATED TRANSFORMED-CELLS

被引:8
作者
COLLETT, MS [1 ]
BELZER, SK [1 ]
KAMP, LE [1 ]
机构
[1] UNIV MINNESOTA, SCH MED, DEPT MICROBIOL, MINNEAPOLIS, MN 55455 USA
关键词
D O I
10.1002/jcb.240260205
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The transforming protein of Rous sarcoma virus (RSV) typically appears as a single phosphorylated polypeptide designated pp60v-src. pp60v-src possesses a protein kinase activity specific for tyrosine residues on select protein substrates. Treatment of RSV-transformed cells with V ions resulted in the appearance of an electrophoretic variant of pp60v-src and was paralleled by a significant increase in the src kinase specific activity in purified enzyme preparations. Both the normal (standard) src kinase and the src kinase preparations obtained from V treated cells exhibited similar optimal activity profiles for MgCl2, KCl and pH. Their site specificities of phosphorylation of the substrates casein and vinculin were the same. The reaction kinetic profile of the standard src kinase showed a nonlinear pattern, while the V enzyme exhibited conventional linear Michaelis-Menten kinetics. These results are discussed with respect to the possible functional regulation of pp60v-src activity by V-sensitive protein phosphatase activity.
引用
收藏
页码:95 / 106
页数:12
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