Prianishnikova E N, Zhulanova Z I, Romantsev E F
Biull Eksp Biol Med. 1983 Feb;95(2):46-8.
Prostaglandin E2 (PGE2) was specifically bound by the membrane fraction prepared from the mouse liver. The binding constants indicate the presence of high-affinity PGE2 binding sites with an apparent dissociation constant (Kd) of 0.82 X 10(-9) M and a capacity of 0.36 X 10(9) M/mg protein and a lower affinity PGE2 binding site with Kd = 15.73 X 10(-9) M and a capacity of 5.31 X 10(9) M/mg protein. The radioprotectors, MEA and APAETP inhibit PGE2 binding and alter its kinetics. Apparently the mechanism of PGE2 binding by membranes is related to interaction of prostaglandins with thiols and sufhydryl groups of membrane lipoproteins, while the radioprotectors modify the functional groups participating in receptor PGE2 binding.
前列腺素E2(PGE2)与从小鼠肝脏制备的膜组分特异性结合。结合常数表明存在高亲和力PGE2结合位点,其表观解离常数(Kd)为0.82×10^(-9) M,容量为0.36×10^9 M/mg蛋白质,以及低亲和力PGE2结合位点,Kd = 15.73×10^(-9) M,容量为5.31×10^9 M/mg蛋白质。辐射防护剂MEA和APAETP抑制PGE2结合并改变其动力学。显然,膜结合PGE2的机制与前列腺素与膜脂蛋白的硫醇和巯基的相互作用有关,而辐射防护剂修饰参与受体PGE2结合的官能团。