抄録
It was presumed that proteinases a, b and c which were separated from the venom of Agkistrodon halys blomhoffii (Mamushi) by DEAE-cellulose chromatography have the different substrate specificities judging from the result of the patterns of the digest of B chain of insulin and glucagon. Some informations about the investigations of the hydrolytic site of B chain of insulin and glucagon with venom proteinase c were presented. B chain of insulin was readily hydrolyzed by proteinase c and the three hydrolytic sites, _??_ and_??_, were identified. The peptides containing arginine or lysine as the C-terminal residue, which are expected to be present in the tryptic digest, were not ob-tained. From the digest of glucagon with venom proteinase c, histidine, serine, phenyla-lanine and leucine were demonstrated as the N-terminal amino acids, and aspartic acid, threonine and presumably tryptophan as the C-terminal residues.
The authors wish to express their gratitude to Dr. T. Murachi of the Department of Biochemistry, Nagoya City University, for the kind supply of precious sample of glucagon. This work was supported, in part, by a grant for scientific researches from the Ministry of Education for “Enzymatic studies on animal toxins”, to which our thanks are due.
