Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus.
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.
Rhodes
J C
JC
Department of Pathology and Laboratory Medicine, University of Cincinnati, College of Medicine, Ohio 45267-0529.
Amlung
T W
TW
Miller
M S
MS
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
D010196:Pancreatic Elastase; D008666:Metalloendopeptidases