Purification and properties of aminopeptidase C from porcine skeletal muscle.

@article{Nishimura1992PurificationAP,
  title={Purification and properties of aminopeptidase C from porcine skeletal muscle.},
  author={Tomonori Nishimura and Yoji Kato and M R Rhyu and Akihiro Okitani and Hiroyuki Kato},
  journal={Comparative biochemistry and physiology. B, Comparative biochemistry},
  year={1992},
  volume={102 1},
  pages={129-35}
}
1. Aminopeptidase C was purified from porcine skeletal muscle. 2. The mol. wt of the enzyme was found to be 103,000 on both Sephadex G-200 column chromatography and SDS-PAGE. 3. The optimum pH for the hydrolysis of L-leucine p-nitroanilide was around 7.0. 4. The activity of this enzyme was strongly inhibited by EDTA, bestatin and puromycin. 5. The enzyme acted on the beta-naphthylamide derivatives of amino acids and oligopeptides. 

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