The amino acid sequence of pancreatic spasmolytic polypeptide

Biochim Biophys Acta. 1985 Mar 1;827(3):410-8. doi: 10.1016/0167-4838(85)90226-2.

Abstract

The sequence of porcine pancreatic spasmolytic polypeptide has been established by a variety of techniques including manual as well as automatic sequencing of fragments resulting from the cleavage of reduced and S-carboxymethylated pancreatic spasmolytic polypeptide with trypsin, chymotrypsin, clostripain, cyanogen bromide and formic acid. The N- and C-terminal sequences were established using pyroglutamate amino-peptidase and carboxypeptidase A, respectively. Pancreatic spasmolytic polypeptide contains 106 amino acid residues in a single chain with seven S-S bridges and a pyroglutamyl blocked N-terminal. The alignment of the sequences representing amino acids 14-49 and 63-98 shows pair-wise identical amino acid residues in 18 out of 36 positions, indicating that these two "domains" have been derived from a common gene.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chymotrypsin / metabolism
  • Cyanogen Bromide
  • Cysteine Endopeptidases*
  • Endopeptidases / metabolism
  • Formates / pharmacology
  • Intercellular Signaling Peptides and Proteins
  • Mucins*
  • Muscle Proteins*
  • Neuropeptides*
  • Peptide Fragments / analysis
  • Peptides / analysis*
  • Pyroglutamyl-Peptidase I / metabolism
  • Swine
  • Trefoil Factor-2
  • Trefoil Factor-3
  • Trypsin / metabolism

Substances

  • Formates
  • Intercellular Signaling Peptides and Proteins
  • Mucins
  • Muscle Proteins
  • Neuropeptides
  • Peptide Fragments
  • Peptides
  • TFF3 protein, rat
  • Tff2 protein, rat
  • Trefoil Factor-2
  • Trefoil Factor-3
  • formic acid
  • pancreatic spasmolytic polypeptide
  • Endopeptidases
  • Pyroglutamyl-Peptidase I
  • Chymotrypsin
  • Trypsin
  • Cysteine Endopeptidases
  • clostripain
  • Cyanogen Bromide