Abstract
Seven wild perennial species were used for characterizing the seed protease inhibitors in the genus Glycine Willd. subgenus Glycine to determine the presence and examine the variability and expression patterns. Seeds of all the species contained trypsin and chymotrypsin inhibitors. There were highly significant variations among the wild perennial species in the electrophoretic profiles of trypsin and chymotrypsin inhibitors, migration patterns of anti-KTI and anti-BBI (mAB 238)immunocrossreactive proteins, and trypsin and chymotrypsin inhibitor activities of seeds
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