Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene.

@article{Matsushita1994PurificationAC,
  title={Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene.},
  author={Osamu Matsushita and K Yoshihara and Seiichi Katayama and Junzaburo Minami and Akinobu Okabe},
  journal={Journal of bacteriology},
  year={1994},
  volume={176 1},
  pages={149-56}
}
Clostridium perfringens type C NCIB 10662 produced various gelatinolytic enzymes with molecular masses ranging from approximately 120 to approximately 80 kDa. A 120-kDa gelatinolytic enzyme was present in the largest quantity in the culture supernatant, and this enzyme was purified to homogeneity on the basis of sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The purified enzyme was identified as the major collagenase of the organism, and it cleaved typical collagenase substrates… CONTINUE READING

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