Premium
Two‐Dimensional Electrophoretic Analysis of Wheat Seed Proteins 1
Author(s) -
Anderson Norman G.,
Tollaksen Sandra L.,
Pascoe Frank H.,
Anderson Leigh
Publication year - 1985
Publication title -
crop science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.76
H-Index - 147
eISSN - 1435-0653
pISSN - 0011-183X
DOI - 10.2135/cropsci1985.0011183x002500040021x
Subject(s) - storage protein , electrophoresis , isoelectric focusing , biology , gel electrophoresis , chromatography , isoelectric point , glutenin , sodium dodecyl sulfate , resolution (logic) , polyacrylamide gel electrophoresis , botany , biochemistry , chemistry , gene , protein subunit , enzyme , artificial intelligence , computer science
High resolution two‐dimenslonal (2‐D) electrophoresis with isoelectric focusing in the first dimension and electrophoresis in sodium dodecyl sulfate in acrylamide gradient gels in the second dimension has been used to produce maps of proteins, including glutenins and gliadins, extracted from wheat seeds. Amino acid substitutions producing single or multiple charge changes, and additions or deletions altering protein mass by approximately 2% are visible on these gels; the former produce horizontal displacements in gel patterns, the latter vertical displacements. The thesis that mutations in storage proteins produce grid patterns of variants on 2‐D gels has been examined experimentally, and confirmatory results have been obtained using 14 varieties of wheat. The results suggest that 2‐D analysis will be useful for varietal identification, for classification of storage proteins of wheat, and for studies un the geneology of wheats.