Powell W S, Hammarström S, Samuelsson B
Eur J Biochem. 1975 Aug 1;56(1):73-7. doi: 10.1111/j.1432-1033.1975.tb02208.x.
Prostaglandin F2alpha was specifically bound by a particulate fraction from bovine corpora lutea. The rate constants for the association (7.5 X 10(3) M-1 S-1) and dissociation (2.1 X 10-4 S-1) reactions gave a dissociation constant of 2.8 X 10(-8) M which is similar to that determined from a Scatchard plot of binding data at equilibrium (5 X 10(-8) M). The receptor was stable for several hours at 23 degrees C but was rapidly destroyed at 37 degrees C. The pH optimum for the binding reaction was 6.3. The receptor had high specificity for prostaglandin F2alpha and had much lower affinities for other prostaglandins. Luteinizing and follicle-stimulating hormones had no effect on the prostaglandin F2alpha-receptor interaction.
前列腺素F2α与牛黄体的微粒体部分特异性结合。结合反应（7.5×10³ M⁻¹ s⁻¹）和解离反应（2.1×10⁻⁴ s⁻¹）的速率常数得出解离常数为2.8×10⁻⁸ M，这与根据平衡结合数据的Scatchard图确定的值（5×10⁻⁸ M）相似。该受体在23℃下稳定数小时，但在37℃下迅速被破坏。结合反应的最适pH为6.3。该受体对前列腺素F2α具有高度特异性，对其他前列腺素的亲和力则低得多。促黄体生成素和促卵泡激素对前列腺素F2α-受体相互作用没有影响。
