Abstract
Previous studies have shown that rabbit antibody-forming cells in the primary and secondary response possess cell-associated antigen-binding receptors. In the present study, we demonstrate that a factor appears in the serum of rabbits following immunization which inhibits the antigen binding of up to 60% of the receptor-bearing antibody-forming cells in both the primary and secondary response. These observations were made on lymph node cells from rabbits primed with either sheep red blood cells (SRBC)3 or 3-nitro-4-hydroxy-5-iodophenylacetic acid coupled to keyhole limpet hemocyanin (NIP-KLH). The inhibitory activity is not associated with anti-SRBC or anti-NIP antibody. In the primary response to SRBC, the antigen binding by day 6 antibody-forming cells is inhibited by the autologous days 7 to 10 inactivated and absorbed serum. In the secondary response to SRBC, the inhibitory factor peaks in the serum around day 10. Later, in both the primary and secondary immune response to SRBC, the inhibitory activity of the serum decreases rapidly. In the primary response to NIP-KLH, the inhibitory activity of the immune sera increased from day 7 through day 14. The receptor-inhibiting factor is antigen specific since the serum from SRBC-primed rabbits inhibits SRBC binding by anti-SRBC antibody-forming cells, but it does not inhibit NIP binding by anti-NIP antibody-forming cells. Similarly, serum from NIP-KLH-primed rabbits inhibits NIP binding by anti-NIP antibody-forming cells, but does not inhibit the SRBC receptor on the anti-SRBC antibody-forming cells. The inhibition is not due to the presence of antihapten or anti-SRBC antibody competing with receptor sites, since the immune sera from one SRBC-primed animal inhibit antigen binding of its own antibody-forming cells, but do not inhibit the antigen binding of antibody-forming cells from other SRBC-primed rabbits.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: 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.