title: Purification of prosomatostatin-converting enzymes.
abstract: The enzymes responsible for performing cleavage of propeptides at basic amino acids have proven difficult to characterize. Using the processing of anglerfish islet prosomatostatin (PSS) as a model system, we are pursuing the characterization of both a single basic amino acid-specific and a dibasic amino acid-specific converting enzyme. We describe here the model system and protein isolation methods that have allowed significant progress toward complete characterization of the somatostatin-generating propeptide converting enzymes (PCEs).
authors.affiliation: Max Planck Research Program, Salk Institute for Biological Studies, La Jolla, CA.
authors.forename: R B
authors.initials: RB
authors.lastname: Mackin
authors.forename: B D
authors.initials: BD
authors.lastname: Noe
authors.forename: J
authors.initials: J
authors.lastname: Spiess
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D005399:Fishes; D007515:Islets of Langerhans / Q000201:enzymology; D008954:Models, Biological; D010447:Peptide Hydrolases / Q000302:isolation & purification*; D011498:Protein Precursors / Q000378:metabolism*; D013004:Somatostatin / Q000378:metabolism*
chemical_list: D011498:Protein Precursors; D013004:Somatostatin; C028456:prosomatostatin; D010447:Peptide Hydrolases