ON SOME AUTOLYZED DERIVATIVES OF BOVINE TRYPSIN

Chromatography or incubation of dilute solutions of bovine trypsin at 4° and pH 5.5 in the presence of Ca2+ appears to induce almost exclusively the autolytic cleavage of bond Arg105-Val106. Bonds Lys49-Ser50 and Lys131-Ser132 are also found substantially autolyzed in commercial trypsin preparations. Evidence is presented suggesting that trypsin still retain activity after cleavage of bonds Arg105-Val106 and Lys131-Ser132. In contrast, the cleavage of bond Lys49-Ser50, close to residue His46, probably inactivates the enzyme. © 1969.