Isolation and characterization of an elastinolytic proteinase from Aspergillus flavus. |
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| Authors: | J C Rhodes T W Amlung M S Miller |
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| Affiliation: | Department of Pathology and Laboratory Medicine, University of Cincinnati, College of Medicine, Ohio 45267-0529. |
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| 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. |
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