Nijs M, Brassinne C, Coune A
Service de Médecine Interne, Institut Jules Bordet, Bruxelles, Belgium.
Cancer Biochem Biophys. 1992 May;12(4):263-74.
Binding of the natural estrogens, estradiol and estriol, was investigated, in 34 samples of human benign prostatic hypertrophy (BPH) tissue, using Scatchard analysis and agar gel electrophoresis. Saturation binding analysis using a wide range of concentrations of both ligands resulted in curvilinear Scatchard plots. This confirmed the presence of two binding forms for estradiol: a true estrogen receptor, and a protein with lower affinity and higher capacity. Both binding species were also demonstrated and quantified with estriol. The electrophoretic process, after incubation at low and high ligand concentrations also resulted in separation, for both estrogens, of two binding peaks. They are probably two distinct forms of the low affinity, high capacity binding measured by Scatchard. The procedure used in our laboratory was not able to provide accurate determination of the concentrations of these binding forms. Possible modifications to alleviate these drawbacks are discussed.
利用Scatchard分析和琼脂凝胶电泳法,对34份人类良性前列腺增生(BPH)组织样本中天然雌激素雌二醇和雌三醇的结合情况进行了研究。使用两种配体的多种浓度进行饱和结合分析,得到了曲线型的Scatchard图。这证实了雌二醇存在两种结合形式:一种是真正的雌激素受体,另一种是亲和力较低但容量较高的蛋白质。两种结合物质也通过雌三醇得到了证实和定量。在低浓度和高浓度配体孵育后进行的电泳过程,也使两种雌激素都分离出了两个结合峰。它们可能是Scatchard法测得的低亲和力、高容量结合的两种不同形式。我们实验室所采用的方法无法准确测定这些结合形式的浓度。文中讨论了可能减轻这些缺点的改进方法。