Isolation and characterization of proSS1-32, a peptide derived from the N-terminal region of porcine preprosomatostatin.
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.
Schmidt
W E
WE
Mutt
V
V
Kratzin
H
H
Carlquist
M
M
Conlon
J M
JM
Creutzfeldt
W
W
D000595:Amino Acid Sequence; D000818:Animals; D002845:Chromatography; D010450:Endopeptidases; D007422:Intestines / Q000032:analysis; D010446:Peptide Fragments / Q000302:isolation & purification*; D011498:Protein Precursors / Q000032:analysis*; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases; D013004:Somatostatin / Q000032:analysis*; D013552:Swine; D014357:Trypsin
D010446:Peptide Fragments; D011498:Protein Precursors; D013004:Somatostatin; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase; D014357:Trypsin