Abstract
Treatment of the rat ovarian membrane-bound and Triton X-100 solubilized LH/hCG receptor with the tryptophan-specific reagents N-bromosuccinimide (NBS) and 2-hydroxy-5-nitrobenzyl bromide (HNB-Br) resulted in inactivation of the receptor to bind hCG. Fluorescence quenching studies indicated that oxidation of tryptophan residues by NBS decreased the accessibility of fluorophores for acrylamide. Preceding binding of hCG to receptor sites was found to protect fluorophores from NBS action. Modification of tryptophan residues was associated with alteration in the rigidity of ovarian membranes and with destabilization of the LH/hCG receptor structure. The results suggest that tryptophan residue is essential for hCG binding to the receptor.
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