title: Characterization of two glycoproteins of human pancreatic juice: P35, a truncated protease E and P19, precursor of protein X.
abstract: Four glycoproteins were separated by SDS-polyacrylamide gel electrophoresis of proteins of human pancreatic juice devoid of free proteolytic activity. The two low molecular weight glycoproteins were isolated and characterized. Protein P19, the precursor family of protein X, was analyzed by its carbohydrate content which seemed to play an important role in protein solubility at pH 8.0. Protein P35 was found to be a Con A-binding protein rich in mannose. Its N-terminal amino acid sequence covering 33 residues revealed a strong homology with human protease E without the dipeptide Val-Val. Is P35 a protein homologous to the subunit III of bovine procarboxypeptidase A?
authors.affiliation: Groupe de Recherche sur les Glandes Exocrines, Marseille, France.
authors.forename: O
authors.initials: O
authors.lastname: Guy-Crotte
authors.forename: C
authors.initials: C
authors.lastname: Barthe
authors.forename: D
authors.initials: D
authors.lastname: Basso
authors.forename: B
authors.initials: B
authors.lastname: Fournet
authors.forename: C
authors.initials: C
authors.lastname: Figarella
mesh_terms: D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins; D002241:Carbohydrates / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D051847:Lithostathine; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010189:Pancreatic Juice / Q000032:analysis* / Q000201:enzymology; D011498:Protein Precursors / Q000302:isolation & purification / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D002135:Calcium-Binding Proteins; D002241:Carbohydrates; D006023:Glycoproteins; D051847:Lithostathine; D011498:Protein Precursors; C497617:REG1A protein, human; D012697:Serine Endopeptidases; C028734:protease E