Lectin-bound alcohol and lactic dehydrogenases as a reagent for the visual detection of glycoproteins.

Alcohol and lactic dehydrogenases were covalently bound to concanavalin A. The conjugates obtained retained their ability to bind glycoprotein as well as to carry out NAD⁺-oxidoreduction in the presence of the appropriate substrates. The dual capacity renders these protein conjugates as a useful reagent for the location of glycoprotein bands on polyacrylamide gels. Visualization of the conjugates absorbed to the glycoprotein is made by precipitation of formazan dye produced as the result of dehydrogenase activity. It is suggested that the present method and its variations may provide a useful analytical tool for histochemical and other detection procedures for glycoconjugates.