Interactions of insolubilized lectins with membrane glycoproteins in presence of detergents

✍ Scribed by M. Dodeur; M.A. Jacquet

• Book ID: 104144940
• Publisher: Elsevier Science
• Year: 1980
• Tongue: English
• Weight: 554 KB
• Volume: 195
• Category: Article
• ISSN: 1873-3778
• DOI: 10.1016/s0021-9673(00)96810-9

✦ Synopsis

The effects of several detergents cummonly used to soiubiiize membrane glycoproteins have been investigated on the binding of hepatoma cell surfaa ~H&akto@ycaproteins to, and their elution from, concanavalin A or f&k&a conz-mu&s k&ins conjugated to Sepharose 4B. The optimum conditions (#I, ionic strength) in the presence of ionic [sodium deoxycholate (DOC) and sodium dodecy1 sulphate (SDS)1 and non-ionic detergents (T&on X-HIO) at a constant concentration were determiued in order to ascertain which would yield the better efficiency. The ef&cts of diflkrent detergent concentrations on binding and elution were then studied. The range of concentrations for each detergent to be used without mod@ing efficiency was determined. Triton X-100 and DOC (0.1-l "A did not change the ettlciency OQ Ricinus ktin-Sepharose, whereas SDS, at a concentration eter than 0.05 %, caused a dramatic decrease in efficiency_ 0n concanavalin A-Sepharose, by contrasf the non-ionic detergent had Rio effect ou tie ef%iciency at all the couceutrations tested (0.1-l %)), while concentrations of more than 0.5 % D0C and 0.1% SDS signikantly decreased both binding and elution.