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
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
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