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Trypsin inhibitors from Pisum sativum L exhibit identical epitopes
Author(s) -
Gaborit Therese,
DelortLaval Jean,
Thanh Luu Phan,
Paraf Alain
Publication year - 1989
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2740480104
Subject(s) - pisum , trypsin , sativum , antiserum , trypsin inhibitor , biochemistry , coomassie brilliant blue , electrophoresis , microbiology and biotechnology , chemistry , chromatography , staining , polyacrylamide gel electrophoresis , gel electrophoresis , polyclonal antibodies , biology , antibody , enzyme , botany , genetics , immunology
Pea ( Pisum sativum L) trypsin inhibitor, known to be a mixture of at least eight different peptides exhibiting different charges as shown by electrophoresis, was subjected to an immunochemical analysis. By PAGE‐SDS analysis, only one large diffuse band was detected showing that pea trypsin inhibitor peptides have a molecular weight between 12000 and 15000 amu. After preparative non‐denaturing electrophoresis, four major bands, as judged by Coomassie blue staining, were purified and each of them was used to raise specific antibodies in rabbits. By ELISA test, immunoelectrophoresis and absorption on an immunoaffinity column, it was shown that each antiserum directed against any one of the four bands completely cross‐reacted against each other. Thus, it can be concluded that each component of the pea trypsin inhibitor should exhibit a very strong sequence homology.