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Preliminary study on isolation, purification and hydrolytic activity of cysteine proteinases in Entamoeba histolytica


Preliminary study on isolation, purification and hydrolytic activity of cysteine proteinases in Entamoeba histolytica



Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi 19(3): 163-165



ISSN/ISBN: 1000-7423

PMID: 12571943

To explore the invading mechanism of amebae in lamina porpria and observe the interaction between the cysteine proteinase (CP) of Entamoeba histolytica and laminin. CP was identified by laminin-sepharose affinity chromatography, followed by isolation, purification and inhibitor experiment. The hydrolytic activity was measured by gelatin electrophoresis. Purified CP of E. histolytica showed a strong affinity with laminin. The molecular weight of CP is 27 kDa. It can be inhibited by EC-64 and exhibited a protein hydrolytic activity. The specific affinity and hydrolytic activity of CP might play an important role in its invasion to the basement membrane of intestinal mucosa.

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Accession: 047046422

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