| Literature DB >> 2115025 |
J C Rhodes1, T W Amlung, M S Miller.
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.Entities:
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Year: 1990 PMID: 2115025 PMCID: PMC258851 DOI: 10.1128/iai.58.8.2529-2534.1990
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441