Undén A, Tatemoto K, Mutt V, Bartfai T
Eur J Biochem. 1984 Dec 17;145(3):525-30. doi: 10.1111/j.1432-1033.1984.tb08588.x.
The specific binding of the chloramine-T iodinated neuropeptide Y (125I-NPY) to membranes from rat cerebral cortex was investigated using equilibrium binding and kinetic methods. The equilibrium binding of 125I-NPY at 37 degrees C was characterized by a Kd value of 0.38 nM. The receptor densities in the cerebral cortex, hypothalamus and cerebellum were 0.45 pmol/mg, 0.47 pmol/mg and 0.04 pmol/mg protein respectively. The binding site for 125I-NPY was sensitive to treatment with proteolytic enzymes and thiol reagents. The binding showed a sharp optimum at pH 7-7.7 and was inhibited by increasing concentrations of Mg2+.
采用平衡结合和动力学方法研究了氯胺 - T碘化神经肽Y（125I - NPY）与大鼠大脑皮质膜的特异性结合。37℃时125I - NPY的平衡结合特征为解离常数（Kd）值为0.38 nM。大脑皮质、下丘脑和小脑中的受体密度分别为0.45 pmol/mg蛋白质、0.47 pmol/mg蛋白质和0.04 pmol/mg蛋白质。125I - NPY的结合位点对蛋白水解酶和硫醇试剂处理敏感。结合在pH 7 - 7.7时显示出明显的最佳值，并受到Mg2 +浓度增加的抑制。
