EFFECT OF SODIUM DODECYL-SULFATE ON CONCANAVALIN A-SEPHAROSE DURING AFFINITY-CHROMATOGRAPHY OF HIGH-AFFINITY BINDING TOXIN PROTEIN OF BACILLUS-THURINGIENSIS SUBSP KURSTAKI

Concanavalin A- Sepharose affinity chromatography is a powerful tool f or isolation or purification of peripheral or integral membrane protei ns or other glycoproteins. The insecticidal crystal toxin from Bacillu s thuringiensis subsp. kurstaki is a glycoprotein containing ''high-ma nnose'' or ''hybrid''- type sugar chains. The protein has a high bindi ng affinity for concanavalin A lectin and could not be eluted even wit h 0.5M methyl alpha-D-mannopyranoside. Nonspecific elution with 0.03% SDS coeluted the matrix con A with bound protein. Experimental results indicated that con A leaching is mainly because of inclusion of deter gents in buffer systems and may not be directly related to the nature of the sample protein.