Interaction of human erythrocyte acetylcholinesterase with lectins

Roberto Ravazzolo, Cecilia Garrè, Franco Ajmar

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 languageEnglish
Pages (from-to)123-126
Number of pages4
JournalScandinavian Journal of Clinical and Laboratory Investigation
Volume43
Issue number2
DOIs
Publication statusPublished - 1983

Fingerprint

Wheat Germ Agglutinins
Acetylcholinesterase
Lectins
Erythrocytes
Concanavalin A
Octoxynol
Erythrocyte Membrane
Phytohemagglutinins
Sepharose
Purification
Membranes
Enzymes

Keywords

  • Acetylcholinesterase
  • Sialic acid
  • Wheat germ lectin

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Interaction of human erythrocyte acetylcholinesterase with lectins. / Ravazzolo, Roberto; Garrè, Cecilia; Ajmar, Franco.

In: Scandinavian Journal of Clinical and Laboratory Investigation, Vol. 43, No. 2, 1983, p. 123-126.

Research output: Contribution to journalArticle

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