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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 adherence protein was purified by acid elution from an immunoaffinity column; however, exposure of the surface membrane...

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Identifiers

PMID: 1578406
DOI: 10.1111/j.1550-7408.1992.tb01322.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Characterization of the galactose-specific binding activity of a purified soluble Entamoeba histolytica adherence lectin.PMID 1578406Read ↗

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