Primary structure of the human pancreatic secretory trypsin inhibitor
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
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Related Subjects
ENZYME INHIBITORS
MOLECULAR STRUCTURE
CHROMATOGRAPHY
HYDROLYSIS
MAN
PANCREAS
PEPTIDES
TRYPSIN
ANIMALS
BODY
CHEMICAL REACTIONS
DECOMPOSITION
DIGESTIVE SYSTEM
ENDOCRINE GLANDS
ENZYMES
GLANDS
HYDROLASES
LYSIS
MAMMALS
ORGANIC COMPOUNDS
ORGANS
PEPTIDE HYDROLASES
PRIMATES
PROTEINS
SEPARATION PROCESSES
SOLVOLYSIS
VERTEBRATES
550200* - Biochemistry