Cross-reactivity of antibodies against synthetic peptides.

Abstract

Antiserum against the synthetic peptide Lys-Arg-Ser-Arg-His-Phe, corresponding to the carboxy terminus of polyoma virus medium tumor antigen (medium T antigen), immunoprecipitates a protein of 36,000 daltons from polyoma virus-infected and uninfected cell extracts treated with the sulfhydryl group reagent N-ethyl-maleimide. This protein appears to share an antigenic determinant with medium T antigen that is normally buried inside the protein or covered up by another protein or cellular structure. The two-dimensional tryptic fingerprints of the 36K protein and of medium T antigen are apparently unrelated to each other. Antiserum against the octapeptide Ac-Met-Asp-Lys-Val-Leu-Asn-Arg-Tyr, including the amino-terminal heptapeptide sequence of the simian virus 40 (SV40) large tumor (T) and small T antigens, cross-reacts with polyoma virus large T antigen, which has an identical amino-terminal heptapeptide sequence except that Lys is replaced by Arg and Asn by Ser. The problem of cross-reactivities of antipeptide sera is discussed.

• Authors: G Walter, H Werchau
• Journal: Journal of cellular biochemistry (J Cell Biochem) Vol. 19 Issue 2 Pg. 119-25 ( 1982) ISSN: 0730-2312 [Print] United States
• PMID: 6294132 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Antibodies
• Antigens, Neoplasm
• Peptides
• Proteins

Topics

• Amino Acid Sequence
• Animals
• Antibodies (immunology)
• Antigens, Neoplasm (immunology)
• Cells, Cultured
• Cross Reactions
• Immunologic Techniques
• Mice
• Peptides (immunology)
• Polyomavirus (immunology)
• Proteins (immunology)
• Simian virus 40 (immunology)