scholarly journals Monoclonal Antibody Specific for Avian Sarcoma Virus Structural Protein p27

1982 ◽  
Vol 62 (2) ◽  
pp. 385-392 ◽  
Author(s):  
N. D. Richert
Keyword(s):  
Monoclonal Antibody ◽  
Structural Protein ◽  
Avian Sarcoma Virus ◽  
Sarcoma Virus ◽  
Avian Sarcoma

Avian sarcoma virus-transformed quail clones defective in the production of focus-forming virus.

1979 ◽  
Vol 30 (1) ◽  
pp. 132-140 ◽  
Author(s):  
W S Mason ◽  
T W Hsu ◽  
C Yeater ◽  
J L Sabran ◽  
G E Mark ◽  
...  
Keyword(s):  
Avian Sarcoma Virus ◽  
Sarcoma Virus ◽  
Avian Sarcoma

Towards a molecular description of cell transformation by avian sarcoma virus

1980 ◽  
Vol 210 (1180) ◽  
pp. 387-396 ◽  
Keyword(s):  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Molecular Mass ◽  
Cellular Protein ◽  
Transformed Cells ◽  
Relative Molecular Mass ◽  
Protein Kinase Activity ◽  
Avian Sarcoma Virus ◽  
Sarcoma Virus ◽  
Avian Sarcoma

The avian sarcoma virus transforming gene product has been identified and partially purified from extracts of transformed cells. It is a phosphoprotein with a relative molecular mass of 60 000 (pp60 src ) with two major sites of phosphorylation. pp60 src appears to be a cyclic-AMP-independent protein kinase as judged by protein phosphorylation with partly purified fractions. The specificity of the phosphorylation observed was judged by inhibition with anti-pp60 src IgG but not by normal IgG and by the fact that the protein kinase activity isolated from ts transformation-mutant infected cells was more thermolabile than that from wild-type transformed cells, thus showing more directly the origin of the enzymic activity. A cellular protein substrate of pp60 src has been identified as a 34000 molecular mass protein. These data together suggest that protein phosphorylation by pp60 src may be a function of the molecule that plays a major role in transformation.

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