Enzymatically active rat liver microsomal antigens with concanavalin A-binding properties

Abstract

By a combination of affinity chromatography and immunoelectrophoretic methods, it was shown that antigens exhibiting several different enzyme activities (nucleoside di- and triphosphatase, NADH-tetrazolium reductase and also in some cases alkaline phosphodiesterase activities), solubilized by detergents from rat liver microsomes, carry sugar moieties that bind to Concanavalin A (Con A) coupled to Sepharose 4B. Similarly, some enzyme active antigens showing only one type of enzyme activity, bind to Con A-Sepharose 4B and can be specifically eluted with α-methyl- d-mannoside. However, two esterase- and two NADH-reductase-active antigens distinct from the multienzyme complexes do not interact with Con A. Thus, Con A binding not only provides a means of characterizing enzyme active antigens as glycoproteins containing certain sugar moieties, but it also gives a simple method for the separation of antigens with similar activities.