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Plasma membrane phosphoproteins in normal and Rous sarcoma virus transformed chick embryo fibroblasts: Characterization by in vitro phosphorylation
Author(s) -
Branton Philip E.,
LandryMagnan Johanne
Publication year - 1979
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041000116
Subject(s) - rous sarcoma virus , phosphorylation , embryo , in vitro , transformation (genetics) , protein phosphorylation , protein kinase a , kinase , biology , endogeny , membrane , microbiology and biotechnology , biochemistry , chemistry , gene
Plasma membranes isolated from normal and RSV transformed chick embryo fibroblasts were phosphorylated in vitro using endogenous protein kinase and ATP (γ 32 P) and the labeled phosphoproteins were analyzed by SDS‐PAGE. A number of protein phosphorylation changes were observed following transformation, however in most cases they were relatively small quantitative differences. The four major changes were in proteins of 47,000, 58,000, 75,000 and 135,000 daltons. Decreased phosphorylation of the 47,000 dalton polypeptide was found in transformed cell membranes but this alteration was shown to be due to differences in cell growth rather than transformation. Increased phosphorylation of the 75,000 dalton protein was at least partially related to virus infection. However, increased phosphorylation of the 58,000 and 135,000 dalton polypeptides were entirely transformation specific.