Abstract
The proteolytic action on α-uroparotin was rather mild for the cleavage of peptide bond except St. griceus protease. Of the biological activities, Ca-activity was unstable against enzymes except B. subtilis proteinase, while L-activity was stable except St. griceus protease. Carbohydrate component of α-uroparotin was distributed into a few polypeptide fragments produced by the enzymatic digestion. Thus, the responsible location for the occurrence of 2 activities was considered to be separated. On the other hand, an active polypeptide may be separated from the digested mixture of α-uroparotin and B. subtilis proteinase.
