TY - JOUR
T1 - Isolation and characterization of proSS1-32, a peptide derived from the N-terminal region of porcine preprosomatostatin
AU - Schmidt, Wolfgang E.
AU - Mutt, Viktor
AU - Kratzin, Hartmut
AU - Carlquist, Mats
AU - Conlon, J. Michael
AU - Creutzfeldt, Werner
N1 - Funding Information:
We thank Professor N. Hilschmann for generous support in performing amino acid analysisa nd J. Friedrich for help with the liquid-phases equencingE. xcellentt echnicala ssistancbey MS E. Rabbe,M S D. Bonhaus,M S D. Michels, MS B. Wehle, Mrs L. Melin and Mrs B. Agerberthi s gratefully acknowledged. This study was supported by Deutsche Forschungsgemeinschaft (grant Cr 20/19-4),t he SwedishM edical Research Council {grant1 3X-01010)S, tiftung Volkswagen-werk and Smith Kline DauelsbergF oundation.
PY - 1985/11/11
Y1 - 1985/11/11
N2 - 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.
AB - 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.
KW - Gastrointestinal peptide
KW - Isolation
KW - N-terminal prosomatostatin peptide
KW - Porcine gut extract
KW - Primary structure Preprosomatostatin processing
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U2 - 10.1016/0014-5793(85)80060-0
DO - 10.1016/0014-5793(85)80060-0
M3 - Article
C2 - 2865169
AN - SCOPUS:0022270680
SN - 0014-5793
VL - 192
SP - 141
EP - 146
JO - FEBS Letters
JF - FEBS Letters
IS - 1
ER -