Association of p21ras with cellular polypeptides

Kaplan, S., Bar-Sagi, D. (October 1991) Association of p21ras with cellular polypeptides. J Biol Chem, 266 (28). pp. 18934-41. ISSN 0021-9258 (Print)0021-9258 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/1918009

Abstract

p21ras specific antiserum was used to immunoprecipitate p21ras polypeptides from human A431 cells. In addition to p21ras, this antiserum precipitated a series of polypeptides with relative molecular weights of 150,000, 120,000, 105,000, and 50,000. The precipitation of these polypeptides was prevented by preincubation of the antiserum with an excess of purified Ras protein. These polypeptides do not share an epitope with p21ras, and two of them (120 and 150 kDa) copurify with a fraction of p21ras. The co-precipitation of p21ras with these polypeptides was detected in a variety of cell types. The pattern of the immunoprecipitates was consistently different in normal and ras-transformed cells. The 120- and 150-kDa polypeptides are phosphorylated on serine and threonine in A431 cells. Serum treatment resulted in a 2-fold increase in the phosphoserine content of the 120-kDa polypeptides.

Item Type: Paper
Uncontrolled Keywords: Animals Antibodies, Monoclonal Cell Line Cell Line, Transformed Electrophoresis, Polyacrylamide Gel Humans Isoelectric Focusing Peptides/*metabolism Precipitin Tests Proto-Oncogene Proteins p21(ras)/immunology/*metabolism Rats
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > G protein > Ras
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: 5 October 1991
Date Deposited: 14 Jan 2016 17:15
Last Modified: 14 Jan 2016 17:15
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32042

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