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Enzymatic characteristics of pp60v‐src isolated from vanadium‐treated transformed cells

Enzymatic characteristics of pp60v‐src isolated from vanadium‐treated transformed cells 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 vanadium 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 vanadium‐treated cells exhibited similar optimal activity profiles for MgCl2, KCl, and pH. Furthermore, 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 vanadium enzyme exhibited conventional linear Michaelis‐Menten kinetics. These results are discussed with respect to the possible functional regulation of pp60v‐src activity by a vanadium‐sensitive protein phosphatase activity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Cellular Biochemistry Wiley

Enzymatic characteristics of pp60v‐src isolated from vanadium‐treated transformed cells

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References (19)

Publisher
Wiley
Copyright
Copyright © 1984 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0730-2312
eISSN
1097-4644
DOI
10.1002/jcb.240260205
pmid
6098587
Publisher site
See Article on Publisher Site

Abstract

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 vanadium 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 vanadium‐treated cells exhibited similar optimal activity profiles for MgCl2, KCl, and pH. Furthermore, 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 vanadium enzyme exhibited conventional linear Michaelis‐Menten kinetics. These results are discussed with respect to the possible functional regulation of pp60v‐src activity by a vanadium‐sensitive protein phosphatase activity.

Journal

Journal of Cellular BiochemistryWiley

Published: Jan 1, 1984

Keywords: ; ; ; ; ;

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