No abstract

Proteins soluble in tris-acetate buffer (pH 9.0) were fractionated by DEAEcellulose, DEAE-Sephadex A-50 and Sephadex G-200 column chromatography. The purified proteins which contained 5-6% carbohydrate, had molecular weights of 125 900 and 22 390 amu. The high molecular weight fraction was homogeneous by polyacrylamide gel electrophoresis. Proteins extracted in phosphate buffer (0.lh1, pH7.6) when subjected to Sephadex G-200 gel chromatography were resolved into three fractions, all of which showed considerable trypsin inhibitor activity. Germination for 3 days reduced the trypsin inhibitor activity of the seed by about 30%.