title: Partial amino acid sequence of human pancreatic stone protein, a novel pancreatic secretory protein.
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.
mesh_terms: D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000032:analysis*; D002137:Calculi / Q000032:analysis*; D002241:Carbohydrates / Q000032:analysis; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007163:Immunosorbent Techniques; D051847:Lithostathine; D009419:Nerve Tissue Proteins; D010189:Pancreatic Juice / Q000032:analysis*; D010758:Phosphorus / Q000032:analysis
chemical_list: D002135:Calcium-Binding Proteins; D002241:Carbohydrates; D051847:Lithostathine; D009419:Nerve Tissue Proteins; C497617:REG1A protein, human; D010758:Phosphorus