CHARACTERIZATION OF POLYCLONAL AND MONOCLONAL ANTIPEPTIDE ANTIBODIES SPECIFIC FOR SOME LOW M(R) SUBUNITS OF WHEAT GLUTENIN AND THEIR USE INTHE DETECTION OF ALLELIC VARIANTS AT GLU-3 LOCI

Citation
S. Denerypapini et al., CHARACTERIZATION OF POLYCLONAL AND MONOCLONAL ANTIPEPTIDE ANTIBODIES SPECIFIC FOR SOME LOW M(R) SUBUNITS OF WHEAT GLUTENIN AND THEIR USE INTHE DETECTION OF ALLELIC VARIANTS AT GLU-3 LOCI, Journal of cereal science, 22(3), 1995, pp. 225-235
Citations number
29
Categorie Soggetti
Food Science & Tenology
Journal title
ISSN journal
07335210
Volume
22
Issue
3
Year of publication
1995
Pages
225 - 235
Database
ISI
SICI code
0733-5210(1995)22:3<225:COPAMA>2.0.ZU;2-4
Abstract
Polyclonal and monoclonal antibodies (Mabs) were produced against the major type of N-terminal amino acid sequence of low M(r) glutenin subu nits. The reactivities of these antibodies were determined using glute nin extracts of several bread wheat cultivars of known allelic composi tion. Analyses were performed by immunoblotting after one or two-dimen sional electrophoresis. One Mab (Mab 6x1) was found to react with low M(r) glutenin subunits encoded by chromosomes 1B and 1D but not with s ubunits controlled by chromosome 1A. Only some of the subunits encoded at the Glu-D3 locus were recognised. In contrast, this Mab reacted wi th all the subunits controlled by the Glu-B3 locus. After single dimen sion SDS-PAGE, we observed significant differences between immunoblot patterns of cultivars expressing different low M(r), glutenin subunits from chromosome 1B. Mab6 xl is a useful reagent for analysing the all elic composition at the Glu-B3 locus. (C) 1995 Academic Press Limited