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Electrophoretic Differences in Seed Proteins among Varieties of Soybean, Glycine max (L.) Merrill 1
Author(s) -
Larsen Arnold L.
Publication year - 1967
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/cropsci1967.0011183x000700040008x
Subject(s) - biology , glycine , polyacrylamide gel electrophoresis , electrophoresis , botany , horticulture , genetics , biochemistry , amino acid , enzyme
Seed proteins of 61 soybean varieties were analyzed by disc electrophoresis. The stained proteins in the polyacrylamide gels revealed two components that separated the varieties into two major groups. Component “A” was present in 13 varieties, and component “B” was present in 48 varieties. In no instance were A and B observed in a single variety. Repeated tests with seed from various environments produced no exceptions to the varietal grouping with respect to these two proteins.