Interaction of human erythrocyte acetylcholinesterase with lectins

Roberto Ravazzolo; Cecilia Garrè; Franco Ajmar

doi:10.1080/00365518309168233

Interaction of human erythrocyte acetylcholinesterase with lectins

Roberto Ravazzolo, Cecilia Garrè, Franco Ajmar

Istituto "Giannina Gaslini"

Research output: Contribution to journal › Article › peer-review

Abstract

Interaction of acetylcholinesterase (AChE) of human erythrocyte membranes with wheat germ lectin, Concanavalin A, Lens Culinaris lectin and phytohaemagglutinin is described. In solutions containing Triton X 100, only Wheat Germ lectin showed significant binding with AChE. Sepharose-immobilized Wheat Germ lectin bound AChE significantly more than Concanavalin A. This interaction was used for partial purification of the enzyme.

Original language	English
Pages (from-to)	123-126
Number of pages	4
Journal	Scandinavian Journal of Clinical and Laboratory Investigation
Volume	43
Issue number	2
DOIs	https://doi.org/10.1080/00365518309168233
Publication status	Published - 1983

Keywords

Acetylcholinesterase
Sialic acid
Wheat germ lectin

ASJC Scopus subject areas

Clinical Biochemistry

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10.1080/00365518309168233

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abstract = "Interaction of acetylcholinesterase (AChE) of human erythrocyte membranes with wheat germ lectin, Concanavalin A, Lens Culinaris lectin and phytohaemagglutinin is described. In solutions containing Triton X 100, only Wheat Germ lectin showed significant binding with AChE. Sepharose-immobilized Wheat Germ lectin bound AChE significantly more than Concanavalin A. This interaction was used for partial purification of the enzyme.",

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AU - Ravazzolo, Roberto

AU - Garrè, Cecilia

AU - Ajmar, Franco

PY - 1983

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N2 - Interaction of acetylcholinesterase (AChE) of human erythrocyte membranes with wheat germ lectin, Concanavalin A, Lens Culinaris lectin and phytohaemagglutinin is described. In solutions containing Triton X 100, only Wheat Germ lectin showed significant binding with AChE. Sepharose-immobilized Wheat Germ lectin bound AChE significantly more than Concanavalin A. This interaction was used for partial purification of the enzyme.

AB - Interaction of acetylcholinesterase (AChE) of human erythrocyte membranes with wheat germ lectin, Concanavalin A, Lens Culinaris lectin and phytohaemagglutinin is described. In solutions containing Triton X 100, only Wheat Germ lectin showed significant binding with AChE. Sepharose-immobilized Wheat Germ lectin bound AChE significantly more than Concanavalin A. This interaction was used for partial purification of the enzyme.

KW - Acetylcholinesterase

KW - Sialic acid

KW - Wheat germ lectin

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