Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus
- Resource Type
- Article
- Authors
- Rhodes, J C; Amlung, T W; Miller, M S
- Source
- Infection and Immunity; August 1990, Vol. 58 Issue: 8 p2529-2534, 6p
- Subject
- Language
- ISSN
- 00199567; 10985522
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.