HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Bunte, T. Articles by Moelling, K. Search for Related Content PubMed PubMed Citation Articles by Bunte, T. Articles by Moelling, K. Agricola Articles by Bunte, T. Articles by Moelling, K.

Analysis of Two Phosphoproteins Related to pp60^src from Schmidt-ruppin D Virus Particles

Max-Planck-Institut für Molekulare Genetik, Ihnestrasse 63-73, D-1000 Berlin 33, F.R.G.

During endogenous phosphorylation of partially purified pp60^src from virus particles, besides pp60^src two additional phosphoproteins, 45K and 42K, were found. These proteins copurify with pp60^src. They were shown to be proteolytic degradation products due to the action of the virus-associated protease p15. All three phosphoproteins were present in particles of two different sarcoma virus strains, Schmidt-Ruppin D and Prague C, indicating that this phenomenon is general rather than strain-specific. The degradation rate of pp60^src was reduced by the presence of 3 mM-ZnCl₂, which acts as a protease inhibitor.

Keywords: Rous sarcoma virus, pp60^src, proteolytic degradation

Received 25 May 1982; accepted 5 October 1982.