Purification and properties of the elastase from Aspergillus fumigatus.

@article{Frosco1992PurificationAP,
  title={Purification and properties of the elastase from Aspergillus fumigatus.},
  author={Marybeth Frosco and ThomasN. Chase and James D. Macmillan},
  journal={Infection and immunity},
  year={1992},
  volume={60 3},
  pages={
          728-34
        }
}
Elastase, a potential virulence factor from the opportunistic pathogen Aspergillus fumigatus, was purified 220-fold from culture broth by fast-performance liquid chromatography employing anion exchange (Q Sepharose fast flow), cation exchange (S Sepharose fast flow), and gel filtration (Superose 12). Purified to near homogeneity, the elastase had an apparent molecular mass of 32 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (silver stain) but a mass of about 19.1 kDa as… CONTINUE READING

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