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Title: Primary structure of the human pancreatic secretory trypsin inhibitor

Journal Article · · Arch. Biochem. Biophys.; (United States)

The amino acid sequence of human pancreatic secretory trypsin inhibitor (Pubols, M. H., Bartelt, D. C., and Greene, L. J. (1974) J. Biol. Chem., 249, 2235-2242) was determined by a combination of selective trypsin and chymotrypsin hydrolysis reactions on the S-2-aminoethylcysteinyl inhibitor and conventional methods (subtractive Edman degradation and expopeptidase hydrolysis) for sequence determination of small peptides. The peptides were ordered on the basis of the identification of the amino- and carboxy-terminal residues of the products at each stage of the degradation procedure. The sequence determination was carried out on a mixture of chromatographic forms present in both tissue and pancreatic juice which are identical in amino acid composition, amino-terminal residues, molecular weight, and specific activity, but differ only in asparagine content and susceptibility to enzymatic hydrolysis. The amino acid sequence of the human inhibitor corresponding to chromatographic form A/sub 3/ has been shown to the NH/sub 2/-Asp-Ser-Leu-Gly-Arg-Glu-Ala-Lys-Cys-Tyr-Asn-Glu-Leu-Asn-Gly-Cys-Thr-Lys-Ile-Tyr-Asn-Pro-Val-Cys-Gly-Thr-Asp-Gly-Asp-Thr-Tyr-Pro-Asn-Glu-Cys-Val-Leu-Cys-Phe-Glu-Asn-Arg-Lys-Arg-Gln-Thr-Ser-Ile-Leu-Ile-Gln-Lys-Ser-Gly-Pro-Cys-COOH. The structure is compared with homologous inhibitors from porcine, bovine, and ovine pancreas.

Research Organization:
Brookhaven National Lab., Upton, NY
OSTI ID:
7321095
Journal Information:
Arch. Biochem. Biophys.; (United States), Vol. 179
Country of Publication:
United States
Language:
English