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Detection and origin of a novel high molecular weight glutenin subunit in hexaploid wild emmer wheat derivatives
Author(s) -
Macgibbon D Bryan,
Porter Noel G
Publication year - 1988
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.2740460106
Subject(s) - glutenin , protein subunit , gel electrophoresis , isoelectric focusing , isoelectric point , polyacrylamide gel electrophoresis , biology , electrophoresis , cultivar , chemistry , biochemistry , botany , gene , enzyme
Several hexaploid derivatives of wild emmer wheat Triticum dicoccoides L developed in Israel possessed a high molecular weight glutenin subunit having slightly lower mobility in sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS‐PAGE) than the Glu‐Ala subunit of the reference cultivar, Hope. The lower mobility subunit appears to have been inherited from the tetraploid wild emmer G25, a parent used in developing the derivatives. Two‐dimensional electrophoresis indicated that the lower mobility subunit from the wild emmer G25 and from the derivatives consisted mainly of two components more basic than the components of the Glu‐Ala subunit from the 20 reference cultivars examined. In 49 wild emmers examined by SDS‐PAGE, at least seven different mobilities were distinguished among the least mobile subunits. Three emmers had a subunit of comparable mobility to the G25 upper band, and one had a subunit of similar mobility to the Glu‐Ala subunit. Two‐dimensional electrophoresis confirmed the match of the former three, but demonstrated a difference between the isoelectric point of the latter and the Glu‐Ala subunit.