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Isolation and characterization of proSS 1–32 , a peptide derived from the N‐terminal region of porcine preprosomatostatin
Author(s) -
Schmidt Wolfgang E.,
Mutt Viktor,
Kratzin Hartmut,
Carlquist Mats,
Conlon J.Michael,
Creutzfeldt Werner
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80060-0
Subject(s) - peptide , peptide sequence , chemistry , cleavage (geology) , stereochemistry , peptide bond , amino acid , peptide fragment , protein primary structure , microbiology and biotechnology , biochemistry , biology , gene , paleontology , fracture (geology)
A peptide derived from the N‐terminal region of porcine prosomatostatin, proSS 1–32 , has been purified to homogeneity from extracts of porcine upper intestine. Amino acid analysis revealed that the peptide consists of 32 residues. The complete primary structure was determined as: A P S D P R L R Q F L Q K S L A A A A G K Q E L A K Y F L A E L This sequence obviously comprises residues 1–32 of porcine prosomatostatin since it is identical to the corresponding sequence in human preprosomatostatin. The postulated cleavage site in porcine prosomatostatin is a Leu‐Leu bond between residues 32 and 33, thus confirming previous studies of the processing of the somatostatin precursor in the rat and transgenic mouse.