Lipshultz L I, Tsai Y H, Sanborn B M, Steinberger E
Fertil Steril. 1977 Sep;28(9):947-51.
The quantitation of androgen-binding activity in human testes, epididymides, and serum is reported and compared with that of similar tissue in the rat. By using steady-state polyacrylamide gel electrophoresis and a tritiated 0.5 nM testosterone label, values for specific binding activity, reported as picomoles per milligram of protein, were found to be 0.21 +/- 0.01 in normal human, epididymides, 0.03 in testes, and 0.44 +/- 0.07 in human serum. Tissues from men receiving exogenous estrogen were also similarly analyzed and found to possess significantly higher androgen-binding activity: 4.10 +/- 0.48 pmoles/mg of protein (epididymides), 4.01 (testes), and 5.63 +/- 1.15 (serum). Since man possesses a sex steroid-binding globulin, attempts were made to differentiate Ion-exchange chromatography, steroid specificity, and dissociation half-time determinations were suggestive but did not conclusively demonstrate the existence of two distinctly different androgen transport macromolecules in man.
本文报道了人睾丸、附睾和血清中雄激素结合活性的定量分析结果,并与大鼠的类似组织进行了比较。通过使用稳态聚丙烯酰胺凝胶电泳和氚标记的0.5 nM睾酮标记物,以每毫克蛋白质的皮摩尔数表示的特异性结合活性值在正常人类附睾中为0.21±0.01,在睾丸中为0.03,在人血清中为0.44±0.07。对接受外源性雌激素的男性的组织也进行了类似分析,发现其雄激素结合活性显著更高:4.10±0.48皮摩尔/毫克蛋白质(附睾)、4.01(睾丸)和5.63±1.15(血清)。由于人类拥有一种性类固醇结合球蛋白,因此尝试进行区分。离子交换色谱法、类固醇特异性和解离半衰期测定具有一定提示性,但并未确凿地证明人类存在两种明显不同的雄激素转运大分子。