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.
Published Version
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
