title: Purification and partial characterization of an elastolytic serine protease of Prevotella intermedia.
abstract: Elastolytic strains of Prevotella intermedia were isolated from pus samples of adult periodontal lesions. Elastase was found to associate with envelope, and it could be solubilized with guanidine-HCl. The enzyme was purified to homogeneity by sequential procedures including ion-exchange chromatography, gel filtration, and hydrophobic interaction chromatography. This elastase was a serine protease, and its mass was 31 kDa. It hydrolyzed elastin powder, but collagen and azodye-conjugated proteins were not degraded by this enzyme. Both synthetic substrates for human pancreatic (glutaryl-L-alanyl-L-alanyl-L-prolyl-L-leucine p-nitroanilide) and leukocyte elastase (methoxy succinyl-L-alanyl-alanyl-L-prolyl-L-valine p-nitroanilide) were hydrolyzed.
authors.affiliation: Department of Oral Microbiology, Matsumoto Dental College, Nagano, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Shibata
authors.forename: S
authors.initials: S
authors.lastname: Fujimura
authors.forename: T
authors.initials: T
authors.lastname: Nakamura
mesh_terms: D006089:Gram-Negative Anaerobic Bacteria / Q000166:cytology / Q000201:enzymology* / Q000254:growth & development; D009842:Oligopeptides / Q000378:metabolism; D010196:Pancreatic Elastase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D010514:Periodontal Pocket / Q000382:microbiology*; D013379:Substrate Specificity
chemical_list: D009842:Oligopeptides; D010196:Pancreatic Elastase