It is now evident that cell surface glycoconjugates play a central role in mediating the social responses of cells. We propose to determine the structure of the carbohydrate moieties of the murine histocompatibility H-2K and H-2D antigens and relate this to the serotype of these glycoproteins. We further propose to explore the interrelationships that may exist among the processes resulting in the stimulation of mitosis and production of Migration Inhibition Factor (MIF), Lymphotoxin, and Chemotactic Factor by perturbation of lymphocyte surface glycoconjugates. Employing sensitive and novel serological, immunochemical and biochemical techniques we will perform partial sequence analysis of both membrane bound and purified H-2K and D antigens to assess the possibility of the influence of primary structure variation of the carbohydrate moiety on the physiologic function of the antigens. These studies will also, by comparing the primary structure of the carbohydrate chains and serotype of various H-2 glycoproteins, assess the possibility of a mechanism which controls and/or links the processes responsible for the biosynthesis of the carbohydrate and polypeptide portions of glycoproteins. Additional studies will be performed to identify molecular species responsible for MIF, LT and ChF activities. Employing a panel of lectins with different lymphocyte receptor specificities, we propose to dissect the individual pathways of lectin induced MIF, LT and ChF by monitoring the appearance of specific molecular species and activities characteristic of these lymphokines.