ON THE MECHANISM OF THE ACTIVATION OF α-CHYMOTRYPSINOGEN TO α-CHYMOTRYPSIN

III. CHROMATOGRAPHIC STUDIES OF THE ACTIVATION OF α-CHYMOTRYPSINOGEN TO α-CHYMOTRYPSIN

Abstract

1. α-Chymotrypsin could be effectively chromatographed on columns of Dowex-50 with 0.1M sodium citrate buffer of pH 6.77, while α-chymotrypsinogen with the same buffer of pH 5.5. The both proteins seem to be chromatographically homogeous, and not to be affected by the procedure.
2. The activation of α-chymotrypsinogen by trypsin was studied chromatographically. The zymogen and two active proteins were separated by the method, and one of the two active proteins seemed to be α-chymotrypsin accompanied with another highly active intermediate protein.
The author wishes to thank professor Shiro Akabori for his guidance through-out this work, and also Mr. Yoshimi 0kada for his valuable technical assistance.