Open AccessCharacterization of a novel anti-peptide antibody that recognizes a specific conformation of the platelet-derived growth factor receptor.
Author(s) -
Subal Bishayee,
Subrata Majumdar,
Charles D. Scher,
Sundas Khan
Publication year - 1988
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.8.9.3696
Subject(s) - autophosphorylation , biology , platelet derived growth factor receptor , peptide , receptor , antibody , microbiology and biotechnology , immunoprecipitation , platelet derived growth factor , peptide sequence , biochemistry , phosphorylation , growth factor , immunology , protein kinase a , gene
Two site-specific anti-peptide antibodies (AbP1 and AbP2) were raised against the platelet-derived growth factor (PDGF) receptor. These two sites correspond to amino acid residues 977 through 988 (peptide 1) and 932 through 947 (peptide 2) of the murine PDGF receptor. Both antibodies recognized human and murine PDGF receptors in immunoprecipitation and immunoblotting analyses. None of the antibodies was directed to phosphotyrosine. One of the antibodies (AbP2) showed unusual antigen recognition specificity. This antibody specifically recognized the tyrosine-phosphorylated PDGF receptor and not the unphosphorylated native receptor, suggesting that recognition by this antibody requires a specific conformation that is induced by PDGF-stimulated autophosphorylation.