Abstract
Two protein proteinase inhibitors, anti-trypsin and anti-chymotrypsin, were isolated from the hemolymph of silkworm larva, Bomby.t nnori, using conventional gel filtration and ion exchange chromatography techniques. They had similar physicochemical properties, in molecular weight (42, 000 for anti-trypsin and 43, 000 for anti-chymotrypsin), in amino acid composition, and in CD spectrum. Further comparison of these characteristics with human serum inhibitors, α-1-proteinase inhibitor and α-1-antichymotrypsin, suggested the resemblance of silkworm and human inhibitors. But the N-terminal sequences were not homologous to each other and antiserum against each silkworm inhibitor only formed a precipitin lines with its own antigen. These results indicated differences in minute parts of the inhibitors.
