Binding of tritiated methylated luteinizing hormone to bovine corpus luteum receptors.
The binding of luteinizing hormone (LH) to cow corpora lutea homogenates was studied using a tritium labelled hormone obtained by reductive methylation. The KD observed was 0.9 10(-10) M and the number of sites was the equivalent of 0.4 10(-15) moles per mg of wet tissue. The influence of the pH and temperature was examined. HCG and LH produced the same binding inhibition properties of the derivative used for labelling LH were similar to those of native LH. The inhibitory activity of the subunits was extremely low (alpha-LH: 4%, beta-LH: 1%). No significant inhibition was observed in the case of FSH or prolactin.
Binding of tritiated methylated luteinizing hormone to bovine corpus luteum receptors. The binding of luteinizing hormone (LH) to cow corpora lutea homogenates was studied using a tritium labelled hormone obtained by reductive methylation. The KD observed was 0.9 10(-10) M and the number of sites was the equivalent of 0.4 10(-15) moles per mg of wet tissue. The influence of the pH and temperature was examined. HCG and LH produced the same binding inhibition properties of the derivative used for labelling LH were similar to those of native LH. The inhibitory activity of the subunits was extremely low (alpha-LH: 4%, beta-LH: 1%). No significant inhibition was observed in the case of FSH or prolactin.