Amino-acid sequences of two basic chymotrypsin inhibitors from silkworm larval hemolymph.
Amino-acid sequences of two basic chymotrypsin inhibitors from silkworm hemolymph (SCI-I and SCI-II) are determined. They are composed of each 62 amino-acid residues with differences in only two positions to each other. They both contain six half cystines in a similar arrangement as that of Kunitz-type proteinase inhibitor, except for the one amino-acid insertion in the first cysteine frame. The inhibitory activity of SCI-II against trypsin should be attributed to Lys44 displacing Gln44 in SCI-I which has no antitryptic activity.
Sasaki
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Department of Food Science and Technology, School of Agriculture, Nagoya University, Aichi, Japan.
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx; D002851:Chromatography, High Pressure Liquid; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D006458:Hemolymph / Q000502:physiology; D007814:Larva; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010447:Peptide Hydrolases; D011480:Protease Inhibitors / Q000302:isolation & purification
D010446:Peptide Fragments; D011480:Protease Inhibitors; D010447:Peptide Hydrolases; D002918:Chymotrypsin