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High affinity monoclonal antibodies to luteinizing hormone-releasing hormone. Preparation and binding studies
Two mouse hybridoma cell lines (50-1 and 50-11) secreting high affinity, monoclonal IgG antibodies (MCAs) against luteinizing hormone-releasing hormone (LHRH) have been established. Measurements of binding affinity by both equilibrium and kinetic methods give dissociation constants (Kd) of 2.3-3.2 X 10(-10) M for 50-1 and 3.0 X 10(-10) M for 50-11. Analysis of binding specificity show that both MCAs require the C-terminal glycine amide and adjacent 4 amino acids of LHRH for binding. The use of these MCAs in radioimmunoassay (RIA) is described.
Two mouse hybridoma cell lines (50-1 and 50-11) secreting high affinity, monoclonal IgG antibodies (MCAs) against luteinizing hormone-releasing hormone (LHRH) have been established. Measurements of binding affinity by both equilibrium and kinetic methods give dissociation constants (Kd) of 2.3-3.2 X 10(-10) M for 50-1 and 3.0 X 10(-10) M for 50-11. Analysis of binding specificity show that both MCAs require the C-terminal glycine amide and adjacent 4 amino acids of LHRH for binding. The use of these MCAs in radioimmunoassay (RIA) is described.
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