High affinity GnRH binding to testicular membrane homogenates |
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Authors: | Marilyn H Perrin Joan M Vaughan Jean E Rivier Wylie W Vale |
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Institution: | Peptide Biology Laboratory The Salk Institute for Biological Studies P.O. Box 85800 San Diego, CA 92138, USA |
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Abstract: | The binding of GnRH to membrane homogenates from collagenase-dissociated normal rat interstitial cells is shown to be of high affinity and specific. The dissociation constant for the radioligand used, 125I-Tyr5, D-Ala6, NαMeLeu7, Pro9-NEt]-GnRH is 0.26 ± 0.02 nM and the number of binding sites is 17 fmoles/mg membrane homogenate. There is one GnRH antagonist whose affinity is greater for the pituitary than for the testis. This antagonist has the same affinity for testis homogenates as for ovarian homogenates. |
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