[Purification and partial characterization of an extracellular aminopeptidase of a collagenolytic bacterium: Empedobacter collagenolyticum].

@article{Montel1982PurificationAP,
  title={[Purification and partial characterization of an extracellular aminopeptidase of a collagenolytic bacterium: Empedobacter collagenolyticum].},
  author={Marie Claude Montel and J. L. Labadie},
  journal={Annales de microbiologie},
  year={1982},
  volume={133 3},
  pages={
          351-63
        }
}
An aminopeptidase was purified from the culture filtrates of a collagenolytic bacterium Empedobacter collagenolyticum. Purification of this enzyme was accomplished by ammonium sulphate precipitation, gel filtration on Sephadex-G200 and chromatography on DEAE-Sephacel. The purified enzyme seemed homogeneous on polyacrylamide gel electrophoresis. The molecular weight of the enzyme was about 100,000 daltons as determined by gel filtration on Sephadex-G200 but it was only 33,000 daltons by disc gel… CONTINUE READING