Purification and characterization of a 27,000-Mr extracellular proteinase from Trichophyton rubrum.

@article{Apodaca1989PurificationAC,
  title={Purification and characterization of a 27,000-Mr extracellular proteinase from Trichophyton rubrum.},
  author={Gerard A. Apodaca and James H McKerrow},
  journal={Infection and immunity},
  year={1989},
  volume={57 10},
  pages={3072-80}
}
A proteinase of Mr 27,000 with a possible role in the metabolism and invasion of host tissues was purified from the conditioned medium of Trichophyton rubrum by concanavalin A and anion-exchange chromatography. Peaks of proteolytic activity were analyzed by substrate gel electrophoresis. The 27,000-Mr proteinase had a pH optimum of 8.0, a calcium dependence of 2 mM, and was inhibited by serine proteinase inhibitors, especially phenylmethylsulfonyl fluoride and Phe-Gly-Ala-Leu-chloromethyl… CONTINUE READING