title: [Preliminary study on isolation, purification and hydrolytic activity of cysteine proteinases in Entamoeba histolytica].
abstract: OBJECTIVE
  To explore the invading mechanism of amebae in lamina porpria and observe the interaction between the cysteine proteinase (CP) of Entamoeba histolytica and laminin.
  
  
  METHODS
  CP was identified by laminin-sepharose affinity chromatography, followed by isolation, purification and inhibitor experiment. The hydrolytic activity was measured by gelatin electrophoresis.
  
  
  RESULTS
  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.
  
  
  CONCLUSIONS
  The specific affinity and hydrolytic activity of CP might play an important role in its invasion to the basement membrane of intestinal mucosa.
authors.affiliation: Department of Biochemistry, Wenzhou Medical College, Wenzhou 325027.
authors.forename: Z
authors.initials: Z
authors.lastname: Yan
authors.forename: S L
authors.initials: SL
authors.lastname: Chen
authors.forename: S Z
authors.initials: SZ
authors.lastname: Mao
mesh_terms: D000818:Animals; D002846:Chromatography, Affinity; D003546:Cysteine Endopeptidases / Q000302:isolation & purification* / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004748:Entamoeba histolytica / Q000201:enzymology*; D007797:Laminin / Q000378:metabolism*
chemical_list: D007797:Laminin; D003546:Cysteine Endopeptidases