ON THE MECHANISM OF THE ACTIVATION OF α-CHYMOTRYPSINOGEN TO α-CHYMOTRYPSIN
IV. THE PEPTIDE LIBERATION DURING ACTIVATION
1956 年 43 巻 4 号 p. 565-574
詳細
1956 年 43 巻 4 号 p. 565-574
1. a-Chymotrypsinogen was activated under dialysis, and the correlation between enzymatic activity and peptide liberation was investigated.
2. In the slow activation, the initial rapid proteolysis was found to be responsible to neither enzymatic activity nor liberation of peptides.
3. The slow activation of a-chymotrypsinogen is accompanied by the formation of several peptides, two of which were identified to be seryl-arginine and threonyl-aspartic acid, and which probably arise from one or two common precursor composed of several amino acid residues.
The author wishes to thank professor Shiro Akabori for his guidance through-out this work, and also Mr. Yoshimi Okada and Miss Hisako Yamada for their valuable technical assistances.
