Entamoeba histolytica: purification of cathepsin B.

@article{Lushbaugh1985EntamoebaHP,
  title={Entamoeba histolytica: purification of cathepsin B.},
  author={William B. Lushbaugh and Alois Hofbauer and Fred E Pittman},
  journal={Experimental parasitology},
  year={1985},
  volume={59 3},
  pages={328-36}
}
A cytotoxic cysteine proteinase with a molecular weight of 16,000 was isolated from axenically grown trophozoites of Entamoeba histolytica. The enzyme was purified from frozen-thawed strain HM-1 by ion-exchange chromatography on DEAE-cellulose, organomercurial agarose affinity chromatography, and size-exclusion chromatography. The purified enzyme had proteinase activity that could be demonstrated on azocasein (pH 5), hemoglobin (pH 5), or carbobenzoxy-L-arginyl--L-arginyl-7-amino-4… CONTINUE READING

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