Abstract
A peptide derived from the N-terminal region of porcine prosomatostatin, proSS1-32, 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.
Original language | English |
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Pages (from-to) | 141-146 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 192 |
Issue number | 1 |
DOIs | |
Publication status | Published (in print/issue) - 11 Nov 1985 |
Keywords
- Gastrointestinal peptide
- Isolation
- N-terminal prosomatostatin peptide
- Porcine gut extract
- Primary structure Preprosomatostatin processing