Complete amino acid sequences of two protease inhibitors in the venom of Bungarus fasciatus.
Two analogous protease inhibitors, VIIIb and IX in the venom of Bungarus fasciatus were reduced and carboxymethylated. Tryptic peptides were separated by cellulose thin-layer peptide mapping technique, and amino acid sequences were analyzed by DABITC/PITC double coupling method. Alignment of all tryptic peptides was established by analyses of chymotryptic peptides and further confirmed by Staphylococcus aureus V8 protease digestion. IX consisted of 65 amino acid residues. VIIIb consisted of 62 residues, identical to the N-terminal 62-amino acid sequence of IX.
D000595:Amino Acid Sequence; D000818:Animals; D002038:Bungarotoxins / Q000032:analysis*; D002918:Chymotrypsin; D007202:Indicators and Reagents; D010446:Peptide Fragments / Q000032:analysis; D011480:Protease Inhibitors / Q000302:isolation & purification*; D012911:Snakes; D014357:Trypsin
D002038:Bungarotoxins; D007202:Indicators and Reagents; D010446:Peptide Fragments; D011480:Protease Inhibitors; D002918:Chymotrypsin; D014357:Trypsin