Studies on the nature of interaction between follicle-stimulating hormone and the testicular receptors.
Two previous reports from this laboratory showed that the binding of 125I-labeled human choriogonadotropin and 125I-labeled human luteinizing hormone to rat testicular receptors is partially irreversible and the binding parameters obtained from Scatchard analysis of the data can be drastically altered simply by changing the reaction volume of the binding assays (Chen, C.J.H., Lindeman, J.G., Trowbridge, C.G. and Bhalla, V.K. (1979) Biochim, Biophys. Acta 584, 407--435; Bhalla, V.K., Trowbridge, C.G., Chen, C.J.H., Lindeman, J.G. and Rojas, F.J. (1979) Biochim, Biophys. Acta 584, 436--453). It is reported herein that the binding reaction between follicle-stimulating hormone and testicular receptors displays very similar characteristics. The results support the previous conclusion that receptor concentrations fluctuate in the membranes and that the extent of their loss from tissue membranes in vitro is dependent upon time and temperature of incubation, the volume of buffer present, and the quantity of hormone used.
D000818:Animals; D001665:Binding Sites; D005640:Follicle Stimulating Hormone / Q000378:metabolism / Q000494:pharmacology*; D007700:Kinetics; D008297:Male; D051381:Rats; D011956:Receptors, Cell Surface / Q000187:drug effects* / Q000378:metabolism; D013737:Testis / Q000187:drug effects* / Q000378:metabolism
D011956:Receptors, Cell Surface; D005640:Follicle Stimulating Hormone