title: Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus.
abstract: An elastinolytic proteinase of Aspergillus flavus has been isolated to homogeneity, and its physical and biochemical properties have been characterized. Two purification protocols were compared; an initial step of ion-exchange chromatography was found to be equivalent to ammonium sulfate precipitation at neutral pH. A combination of gel filtration and adsorption chromatographies on the resultant crude enzyme produced highly purified elastase with yields of 5 to 10%. The enzyme is a 23-kilodalton protein with a pI of 7.6. The enzyme activity is markedly inhibited by numerous metal ions. Aspergillus elastase appears to be a metalloproteinase EC 3.4.24.X), as determined by its sensitivity to 1,10-phenanthroline.
authors.affiliation: Department of Pathology and Laboratory Medicine, University of Cincinnati, College of Medicine, Ohio 45267-0529.
authors.forename: J C
authors.initials: JC
authors.lastname: Rhodes
authors.forename: T W
authors.initials: TW
authors.lastname: Amlung
authors.forename: M S
authors.initials: MS
authors.lastname: Miller
mesh_terms: D001231:Aspergillus flavus / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007526:Isoelectric Point; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism; D008970:Molecular Weight; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature
chemical_list: D010196:Pancreatic Elastase; D008666:Metalloendopeptidases