title: Bovine pancreatic elastase II cleaves Gln-Ile bond.
abstract: A peptidase (GICP) that cleaves the Gln-Ile bond of a peptide Gly-Ile-Asp-Val-Gln-Ile-Tyr(T-1), a sequence in phenylalanine oxidase, was purified from bovine pancreas. The purified enzyme had an Mr of approximately 29,000, as determined by SDS-PAGE, and its N-terminal sequence was identical to that of bovine pancreatic elastase II. The enzyme released Gly-Ile-Asp-Val-Gln and Ile-Tyr from T-1 (Km = 8.3 microM k(cat) = 2.1 s(-1)) and the catalytic efficiency (2.6 X 10(5) M(-1)s(-1)) was comparable to those of elastase II from porcine pancreas and rat mesenteric arterial bed perfusate. The P1 site specificity of GICP toward oxidized insulin A and B chains suggested that major cleavage sites were the peptide bond at the C-terminal side of Gln, Leu, His, and Tyr residues.
authors.affiliation: Division of Biosciences, Graduate School of Fundamental Life Science, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Azuma
authors.forename: Y
authors.initials: Y
authors.lastname: Banshou
authors.forename: H
authors.initials: H
authors.lastname: Suzuki
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007328:Insulin / Q000737:chemistry / Q000378:metabolism; D008670:Metals / Q000494:pharmacology; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology*; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology; D013379:Substrate Specificity; D013997:Time Factors
chemical_list: D007328:Insulin; D008670:Metals; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; C117309:pancreatic elastase II