Further Studies on the Distribution of Trypsin Inhibitors in the Proteins of Various Avian Egg Whites I. Distribution of Trypsin Inhibiting Activities in tie Chicken Egg White Proteins

Chicken egg white was separated into protein fractions by electrophoresis on a square sheet of filter paper. Then bovine trypsin was applied on a line perpendicular to the zones of the egg white proteins and the second electrophoresis was carried out in the direction perpendicular to the first run. In this way trypsin line crossed the zones of egg white proteins. Following results were obtained. 1) Trypsin line formed two peaks by the cross with the fractions of the chicken egg white. The major peak was ascribed to the crossing of ovomucoid and the second minor one, to that of conalbumin. 2) Trypsin inhibiting activity of each fraction isolated by sectioning the paper electropherogram was measured using benzoylarginine p-nitroanilide and chymotrypsin inhibiting activity was measured using benzoyltyrosine p-nitroanilide. 3) The distribution curves of trypsin inhibitors measured enzymatically coincided with the curve of trypsin line which was crossed the egg white proteins and named the cross diagram of the chicken egg white against trypsin. 4) The peak of chymotrypsin inhibitor in the distribution curve corresponded to the minor second peak of the cross diagram against trypsin.