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Biochemical Journal logoLink to Biochemical Journal
. 1986 Aug 15;238(1):227–232. doi: 10.1042/bj2380227

Partial amino acid sequence of human pancreatic stone protein, a novel pancreatic secretory protein.

G Montalto, J Bonicel, L Multigner, M Rovery, H Sarles, A De Caro
PMCID: PMC1147119  PMID: 3541906

Abstract

Pancreatic stone protein (PSP) is the major organic component of human pancreatic stones. With the use of monoclonal antibody immunoadsorbents, five immunoreactive forms (PSP-S) with close Mr values (14,000-19,000) were isolated from normal pancreatic juice. By CM-Trisacryl M chromatography the lowest-Mr form (PSP-S1) was separated from the others and some of its molecular characteristics were investigated. The Mr of the PSP-S1 polypeptide chain calculated from the amino acid composition was about 16,100. The N-terminal sequences (40 residues) of PSP and PSP-S1 are identical, which suggests that the peptide backbone is the same for both of these polypeptides. The PSP-S1 sequence was determined up to residue 65 and was found to be different from all other known protein sequences.

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Selected References

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