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The acid-soluble whey proteins from seeds of several varieties of soybeans were analyzed by disc electrophoresis. Almost all varieties had a very intense protein band just behind the front which corresponded with the major band of commercial soybean trypsin inhibitor. The lines L63-9485 and T-245 lacked this band, but had a slightly slower moving band. The F1 seed of reciprocal crosses between L63-9485 and Clark possessed both intense bands, while the F2 seed segregated to show one or the other or both bands. The gels were sliced and extracted with buffer. Trypsin inhibitor was recovered from the area of both intensely stained bands.
Key Words: Glycine max (L.) Merr.
2 Rockefeller Foundation Fellow in Plant Genetics; Research Chemist, Crops Research Division, ARS, USDA; and Professor of Plant Genetics, University of Illinois, Urbana, Illinois, repectively.
Received for publication February 5, 1969.
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