This investigation was primarily concerned with the interaction of the ('125)I-labeled human gonadotropins with testicular tissue from the human and from nonhuman primate species. The binding of the ('125)I-hFSH and ('125)I-hCG (or ('125)I-hLH) to a particulate fraction (P1) of the primate testis was highly specific. Gonadotropin binding was competitively displaced by the synthetic estrogens and an inhibitory factor present in testicular extracts (140,000 x g supernatant). The biochemical properties of the gonadotropin receptor (testicular) interaction of the different primate species were similar in most respects. All tissues had a greater FSH than LH binding capacity with an apparent dissociation constant in the range of 10('-10)-10('-11)M. / An FSH responsive adenylyl cyclase was characterized in human testicular membranes. In the presence of a chemically deglycosylated derivative of FSH it was possible to uncouple the FSH responsive adenylate cyclase system. The synthetic estrogens were also effective inhibitors of the human testicular adenylyl cyclase.
| Identifer | oai:union.ndltd.org:LACETR/oai:collectionscanada.gc.ca:QMM.71864 |
| Date | January 1984 |
| Creators | Berman, Marvin. |
| Publisher | McGill University |
| Source Sets | Library and Archives Canada ETDs Repository / Centre d'archives des thèses électroniques de Bibliothèque et Archives Canada |
| Language | English |
| Detected Language | English |
| Type | Electronic Thesis or Dissertation |
| Format | application/pdf |
| Coverage | Doctor of Philosophy (Department of Physiology.) |
| Rights | All items in eScholarship@McGill are protected by copyright with all rights reserved unless otherwise indicated. |
| Relation | alephsysno: 000218659, proquestno: AAINK66583, Theses scanned by UMI/ProQuest. |
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