Binding of acetylcholinesterases to concanavalin A.

摘要: Acetylcholinesterases from a number of different sources are known to be glycoproteins. Carbohydrate residues were found in the eel enzyme [ 1,2] , human erythrocyte acetylcholinesterase [3 ] torpedo California [4] plaice cholinesterase 51 and cholinesterases serum [6,7], horse [8,9] brain [lo]. It was interest us examine whether presence carbohydrate would yield specific interaction between plant lectin concanavalin A (con-A) acetylcholinesterases. Such interactions recently shown with crantitrypsin 1 l] /3-galactosidase 121 dopaine+ hydroxylase 131. This paper presents evidence that acetylcholinesterases erythrocytes, electric organ Electrophoms electricus body muscle bound columns con-Asepharose selectively eluted by o-methyl-Dmannoside. The complex formed con-A could demonstrated gel filtration on sepharose 4B. separated aqueous phase which reextracted twice toluene. combined quarkphases above buffer. extracts centrifuged again for 30 min at 20 000 g. They contained 87% total activity. Sucrose density gradient centrifugation showed this treatment only elongated forms A, C D obtained. Form G, proteolytic breakdown product forms, not detected. As source form commercially available (Sigma Type VI) used. Human prepared as described previously 161 gift Dr S. J. Lundin. Con-A, con-A-sepharose 4B obtained Pharmacia (Sweden). o-Methyl-Dmannoside, acetylthiocholine 5,5dithio nitrobenzoic acid purchased Fluka. All other chemicals reagent grade. Acetylcholinesterase activity determined 30°C following production thiocholine according method Ellman et al. 171.