Cleavage of the ArgIle bond in the native polypeptide chain of human pancreatic stone protein
- 1 June 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 216 (2), 195-199
- https://doi.org/10.1016/0014-5793(87)80688-9
Abstract
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 CaCO3-crystal growth in pancreatic juice. PSP and PSP S1 N-terminal sequences are identical (NH2Ile-). 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.Keywords
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