Gonadotropin receptors in human corpora lutea of the menstrual cycle and pregnancy.
Binding of 125I-human choriogonadotropin (hCG) to homogenates of corpora lutea of the menstrual cycle and pregnancy was examined. While corpora lutea of the menstrual cycle bound 125I-hCG, most of the corpora lutea of pregnancy from six to 34 weeks' gestation bound little or none of the added 125 I-hCG. Further exploration into various possibilities for the above findings led to the conclusion that these corpora lutea either contain very few gonadotropin receptors or lack them altogether. The selected properties of gonadotropin receptors in corpora lutea of the cycle were studied. The apparent dissociation constant for binding was about the same (2.6 to 3.8 x 10-10M) in all but one corpus luteum. In this one sample the constant was three- to five-fold higher (1.3 x 10-9M). The binding was quite rapid and reversible, and it exhibited dependence on the amount of 125I-hCG, homogenate protein, pH of the incubation media, and duration of incubation. hCG and human lutropin (hLH') competed for 125I-hCG binding, but hCG subunits (alpha and beta), human follitropin, and ovine prolactin did not. Although hCG and hLH were parallel in inhibiting 125I-hCG binding, hLH was found to be relatively less effective. The studies with various enzymes revealed that gonadotropin receptors are protein in nature.
Gonadotropin receptors in human corpora lutea of the menstrual cycle and pregnancy. Binding of 125I-human choriogonadotropin (hCG) to homogenates of corpora lutea of the menstrual cycle and pregnancy was examined. While corpora lutea of the menstrual cycle bound 125I-hCG, most of the corpora lutea of pregnancy from six to 34 weeks' gestation bound little or none of the added 125 I-hCG. Further exploration into various possibilities for the above findings led to the conclusion that these corpora lutea either contain very few gonadotropin receptors or lack them altogether. The selected properties of gonadotropin receptors in corpora lutea of the cycle were studied. The apparent dissociation constant for binding was about the same (2.6 to 3.8 x 10-10M) in all but one corpus luteum. In this one sample the constant was three- to five-fold higher (1.3 x 10-9M). The binding was quite rapid and reversible, and it exhibited dependence on the amount of 125I-hCG, homogenate protein, pH of the incubation media, and duration of incubation. hCG and human lutropin (hLH') competed for 125I-hCG binding, but hCG subunits (alpha and beta), human follitropin, and ovine prolactin did not. Although hCG and hLH were parallel in inhibiting 125I-hCG binding, hLH was found to be relatively less effective. The studies with various enzymes revealed that gonadotropin receptors are protein in nature.