Abstract
The primary structure of Vipera ammodytes venom trypsin inhibitor I consists of 61 amino acid residues in the sequence: Pyr-Asp-His-Pro-Lys-Phe-Cys-Tyr-Leu-Pro-Ala-Asp-Pro-Gly-Arg-Cys-Lys-Ala-His-Ile- Pro-Arg-Phe-Tyr-Tyr-Asp-Ser-Ala-Ser-Asn-Lys-Cys-Asn-Lys-Phe-Ile-Tyr-Gly-Gly-Cys-Pro-Gly-Asn-Ala- Asn-Asn-Phe-Lys-Thr-Trp-Asp-Glu-Cys-Arg-Gln-Thr-Cys-Gly-Ala-Ser-Ala. The N-terminal group of the inhibitor is pyrrolidonecarboxylic acid. The sequential data were obtained by analysis of peptides isolated from tryptic and chymotryptic digests and by analysis of peptides derived from the hydrolysis of the aspartyl-prolyl bond of the carboxymethylated inhibitor. The primary structure of trypsin inhibitor I presented shows approximately 80% sequence homology with chymotrypsin inhibitor isolated from the venom of the same snake, and nearly 50% homology with bovine basic pancreatic trypsin inhibitor. It belongs to the Kunitz-pancreatic trypsin inhibitor family of inhibitors.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
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