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.
|Number of pages||4|
|Journal||Scandinavian Journal of Clinical and Laboratory Investigation|
|Publication status||Published - 1983|
- Sialic acid
- Wheat germ lectin
ASJC Scopus subject areas
- Clinical Biochemistry