Abstract
The initial observations of LH receptor binding inhibitor activity were quite serendipitous. A graduate student (Dr. Kuo-Pao Paul Yang) attempted to use some ovaries from psuedopregnant rats as a source of receptors for luteinizing hormone. These ovaries had been stored for quite some time at -20°. When Paul attempted to measure LH-binding in a crude homogenate of these ovaries no significant binding was observed. However, in the residuum after 1,2 or 3 washings there was significant specific binding for LH. Our first studies (Yang et al., 1976a) demonstrated that the binding inhibition resided in both a low molecular weight (dialyzable) and a high molecular weight (non-dializable) fraction. We were aware of the earlier studies of Bhalla and Reichert (1974) concerning an aqueous ethanol solubilized fraction from testicular tissue which interacted directly with gonadotropins as shown by physical properties. Reichert and Bhalla had suggested the material behaved as though it were a solubilized portion of the hormone receptor. We demonstrated, at least for the low molecular weight form of the LH.RBI, that such a direct interaction of our material with LH was not obtained.
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© 1982 Plenum Press, New York
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Ward, D.N., Liu, WK., Glenn, S.D., Channing, C.P. (1982). LH-Binding Inhibitors from the Corpus Luteum. In: Channing, C.P., Segal, S.J. (eds) Intraovarian Control Mechanisms. Advances in Experimental Medicine and Biology, vol 147. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-9278-5_15
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DOI: https://doi.org/10.1007/978-1-4615-9278-5_15
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