The reactive site of silkworm hemolymph antichymotrypsin is located at the COOH-terminal region of the molecule.
The complex of silkworm larval hemolymph antichymotrypsin (Mr = 43,000) and C-chain of bovine alpha-chymotrypsin was obtained. This complex showed two NH2-terminal amino acid sequences identical to those of intact silkworm antichymotrypsin and C-chain of alpha-chymotrypsin, respectively. Alkali treatment of the complex brought about its dissociation and the separated inhibitor component (Mr = 36,000) had an NH2-terminal amino acid sequence identical to that of intact silkworm antichymotrypsin. These results suggest that the reactive site of this inhibitor is located at the COOH-terminal region of the molecule and that the nature of association of this inhibitor and alpha-chymotrypsin is an acyl-bond.
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D012831:Bombyx; D002918:Chymotrypsin / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D006458:Hemolymph / Q000032:analysis*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D000514:alpha 1-Antichymotrypsin
D000514:alpha 1-Antichymotrypsin; D002918:Chymotrypsin