PARTIAL CHARACTERIZATION OF AN INHIBITOR OF PROTEIN-SYNTHESIS IN RABBIT ERYTHROCYTES - ITS RELATIONSHIP TO THE OXIDATIVE STRESS ACTIVATED INHIBITOR IN RABBIT RETICULOCYTES

An inhibitor of protein synthesis has been shown to be activated in in rabbit reticulocytes under various stress conditions like high oxygen partial pressure, presence of glutathione disulfide or heat treatment (1). Glucose-6-phosphate prevents this activation. The present study shows that a related inhibitor is present in rabbit erythrocytes in an active state already without exerted stress. The activation of the inhibitor is discussed in terms of its possible role in the final erythrocyte maturation

Immune response to progesterone involved in Cu2+-mediated polyanion-protein complex - Antigen specificity and affinity of hybridoma clones

The immunogenic properties of water soluble (PAA-Cu2+-BSA) and colloidal (PAA-Cu2+-BSA.P) polycomplexes were investigated, and the specificity of antibodies produced was analyzed. Polycomplexes containing progesterone appeared to possess a high steroid-specific immunogenic activity. A comparative study of immunogenic properties of polycomplexes versus BSA.P + incomplete Freund's adjuvant (IFA) mixtures revealed differences in regards to the specificity of antibody production. In contrast to the IFA system, polycomplexes were able to generate P- as well as BSA-specific antibodies. Such a response is determined, possibly, by increases in the immunogenicity of weak antigenic determinants on the surface of protein globules and/or by the representation of 'dormant' determinants existing in the inner site upon complex formation with polyelectrolytes. Finally, using a short immunization procedure based on use of PAA-Cu2+-BSA polycomplexes, we produced seven monoclonal antibodies against progesterone included in polyelectrolyte complexes with affinities K-d ranging between 1.3 x 10(-7) and 9 x 10(-8) M