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Cross‐reactivity of antibodies against synthetic peptides
Author(s) -
Walter Gernot,
Werchau Hermann
Publication year - 1982
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240190203
Subject(s) - antiserum , antigen , antibody , peptide , microbiology and biotechnology , biology , peptide sequence , virus , amino acid , virology , biochemistry , immunology , gene
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.