Article
Characterization of the galactose-specific binding activity of a purified soluble Entamoeba histolytica adherence lectin.
The Journal of protozoology - 1 Jan 2000
Ravdin J I, Murphy C F
Abstract excerpt
We studied galactose (Gal)-specific binding of the soluble purified 260-kDa Entamoeba histolytica adherence protein to glycosylation deficient Chinese hamster ovary (CHO) cell mutants. Our goal was to further define the lectin's functional activity and carbohydrate receptor specificity. The adher...
Topics
- Animals
- CHO Cells
- Chromatography, Affinity
- Cricetinae
- Entamoeba histolytica
- Galactose
- Lectins
- Mutation
- Radioimmunoassay
