Polarographic Waves of Soybean Proteins Fractionated by Gel Filtration with Sephadex G-200 Column

Abstract

Water-extractable soybean proteins were fractionated into four fractions by gel filtration with Sephadex G-200 column. The properties of these four fractions were investigated by trypsin digestion, and by paper electrophoresis. Comparative studies were also made on the polarographic protein waves of the fractions. Marked difference was observed in polarographic behaviors between the fraction which contained all the trypsin inhibitive activity in the water-extractable soybean proteins and the other three fractions which had no activity.