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Cleavage of the ArgIle bond in the native polypeptide chain of human pancreatic stone protein
Author(s) -
Rouimi P.,
Bonicel J.,
Rovery M.,
De Caro A.
Publication year - 1987
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(87)80688-9
Subject(s) - polypeptide chain , chemistry , cleavage (geology) , biochemistry , pancreatic polypeptide , stereochemistry , microbiology and biotechnology , biology , amino acid , paleontology , fracture (geology) , glucagon , hormone
The pancreatic stone protein (PSP) isolated from calculi ( M r 14000) and the 5 protein forms (PSP S1‐5) detected in pancreatic juice ( M r 14000—19000) derive from the same source differing seemingly in their carbohydrate contents or/and in their polypeptidic chain lengths. This kind of protein would inhibit in vivo CaCO 3 ‐crystal growth in pancreatic juice. PSP and PSP S1 N‐terminal sequences are identical (NH 2 Ile‐). This report demonstrates that: (i) in PSP S2‐5 the amino‐terminal is blocked; (ii) the C‐terminus is alike in every form; (iii) the single polypeptide chain of PSP S2‐5 is converted into that of PSP S1 or PSP by the specific trypsin cleavage of the ArgIle bond.