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Amino acid sequence of a novel Kunitz‐type chymotrypsin inhibitor from hemolymph of silkworm larvae, Bombyx mori
Author(s) -
Sasaki Takuji
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80251-3
Subject(s) - bombyx mori , chymotrypsin , biochemistry , hemolymph , trypsin , trypsin inhibitor , bombycidae , peptide sequence , amino acid , kunitz sti protease inhibitor , protein primary structure , chemistry , microbiology and biotechnology , biology , enzyme , gene
The primary structure of the chymotrypsin inhibitor (SCI‐III), from larvae of the silkworm, Bombyx mori , has been determined. This inhibitor seems to be a Kunitz‐type inhibitor judging from the sequence homology with the bovine basic pancreatic trypsin inhibitor, but has one more amino acid in the half‐cystine frame nearest the N‐terminus. The amino acid at the deduced reactive site (P 1 ) is phenylalanine and this inhibitor is the first example of the Kunitz type that is assigned phenylalanine to its reactive site.