Abstract
Antibodies against synthetic peptides corresponding to the carboxyl-terminal six amino acids, Lys-Arg-Ser-Arg-His-Phe (KF), and an internal region, Glu-Glu-Glu-Glu-Tyr-Met-Pro-Met-Glu (EE), of polyoma virus medium T antigen were used successively to purify medium T antigen by affinity chromatography. Medium T antigen from cell extracts was first bound to anti-KF antibodies and released from the immune complex with excess KF peptide; then it was bound to anti-EE antibodies and released with excess EE peptide. Two proteins, pp60c-src and a new protein of approximately equal to 61,000 Da (61-kDa protein), were copurified because they formed complexes with medium T antigen. The 61-kDa protein-medium T antigen complex was detected in extracts from wild-type-infected and transformed cells but not from cells infected with NG59 virus, which has a mutation in the medium T gene and is transformation defective. Instead, NG59 medium T antigen formed a complex with another cellular protein of approximately equal to 72,000 Da.
MeSH Terms
Animals
Antigens, Viral, Tumor
Immunosorbent Techniques
Macromolecular Substances
Mice
Molecular Weight
Polyomavirus/immunology,metabolism
Protein Binding
Proteins/metabolism
Proto-Oncogene Proteins/metabolism
Proto-Oncogene Proteins pp60(c-src)
Viral Proteins/metabolism
Chemicals
Antigens, Viral, Tumor
Macromolecular Substances
Proteins
Proto-Oncogene Proteins
Viral Proteins
Proto-Oncogene Proteins pp60(c-src)
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Grussenmeyer T
Scheidtmann K H
Hutchinson M A
Eckhart W
Walter G
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