A human chorionic gonadotropin-specific antiserum against synthetic peptide analogs to the carboxyl-terminal peptide of its beta-subunit.

A chemically synthesized Na-acetyl-triacontapeptide analogous to the carboxyl-terminal region (residues 116--145) of hCG beta-subunit was conjugated to bovine thyroglobulin. This synthetic antigen was used to immunize five rabbits; one of these rabbits (H-114) generated a useable antiserum. The binding properties of this antiserum were compared extensively to a well characterized antiserum (H-93) against the natural tricosaglycopeptide (residues 123--145) of desialylated hCG beta-subunit conjugated to bovine serum albumin. The two antisera showed nearly identical immunological specificities and sensitivities when examined in a conventional RIA system. These similarities included: 1) antibody recognition sites residing at the carboxyl-terminal pentadecapeptide region; 2) binding neither [125I]iodo-hLH nor [125I]iodo-oLH; and 3) lack of neutralizing capability against the biological activity of hCG in vivo. However, synthetic pentadeca or longer peptides are twice as potent in inhibiting 125I]iodo-hCG binding to H-114 than to H-93. Synthetic peptides may provide a superior means of generating antisera capable of distinguishing hCG from human LH, since they can be obtained more easily in large quantities than analogous purified natural fragments and because peptides of synthetic origin avoid the risk of contamination from strongly antigenic regions of the native molecules. Such hCG-specific antisera may have extensive application in RIA systems and fertility control, where selective binding to hCG but not human LH is desired.