In:
FEBS Letters, Wiley, Vol. 192, No. 1 ( 1985-11-11), p. 141-146
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(85)80060-0
Language:
English
Publisher:
Wiley
Publication Date:
1985
detail.hit.zdb_id:
1460391-3
SSG:
12
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