THE BINDING OF LARGE MOLECULAR MASS PROCYANIDINS FROM BIRD RESISTANT SORGHUM GRAIN TO SOLUBLE-PROTEINS

1. The relative strength of the interactions between procyanidin and five water soluble proteins (bovine serum albumin and hemoglobin, trypsin, pepsin and protamine) of widely different isoelectric points was measured at pH 5.0 and an ionic strength of 0. 1. 2. The only protein feature that explained the variation in binding was the total positive charge donated by the amino acids lysine, arginine and histidine.