Isolation and characterization of proSS1–32, a peptide derived from the N‐terminal region of porcine preprosomatostatin

FEBS Letters

Kratzin, Hartmut²  Mutt, Viktor³  Carlquist, Mats³  Creutzfeldt, Werner¹  Conlon, J.Michael⁴  Schmidt, Wolfgang E.¹ 

[1] Division of Gastroenterology and Metabolism, Department of Medicine, University of Göttingen, D-3400 Göttingen, FRG;Department of Immunochemistry, Max-Planck-Institute for Experimental Medicine, Göttingen, FRG;Department of Biochemistry II, Medical Nobel Institute, Karolinska Institute, Stockholm, Sweden;Clinical Research Group for Gastrointestinal Endocrinology of the Max-Planck-Society at the Department of Medicine, University of Göttingen, FRG

关键词: N-terminal prosomatostatin peptide;    Isolation;    Porcine gut extract;    Primary structure Preprosomatostatin processing;    Gastrointestinal peptide;   

DOI  :  10.1016/0014-5793(85)80060-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown