Arányi P
Eur J Biochem. 1983 Jan 1;129(3):549-54. doi: 10.1111/j.1432-1033.1983.tb07084.x.
Cytosol glucocorticoid receptors acquired the ability to bind to DNA-cellulose on incubation at 25-37 degrees C and/or in media of high ionic strength (0.3 M KCl). However, this activation was transient only. It was followed by deactivation whose rate was also dependent on incubation temperature and on the presence of potassium chloride. Deactivation resulted in a decreased but non-zero binding to DNA-cellulose. Specific triamcinolone acetonide binding to the receptor protein was not lost under the same conditions. Deactivation commenced before it became apparent, probably together with activation. Preactivated complex underwent deactivation even in conditions that would not allow significant decrease in DNA-cellulose binding without previous incubation at 37 degrees C. In contrast to previous reports it was found that fast activation/deactivation took place in the presence of 4 mM Ca2+. Molybdate ions slow down both activation and deactivation, but do not prevent activation by heat. Heat activated/deactivated complex differed in size from both non-activated and Ca2+-deactivated complexes. This finding suggests that heat and Ca2+-induced deactivation follow different mechanisms.
胞质溶胶糖皮质激素受体在25 - 37摄氏度孵育和/或在高离子强度（0.3M KCl）介质中时获得了与DNA纤维素结合的能力。然而，这种激活只是短暂的。随后是失活，其速率也取决于孵育温度和氯化钾的存在。失活导致与DNA纤维素的结合减少但不为零。在相同条件下，特异性曲安奈德与受体蛋白的结合并未丧失。失活在变得明显之前就开始了，可能与激活同时发生。即使在没有事先在37摄氏度孵育就不会使DNA纤维素结合显著减少的条件下，预激活的复合物也会发生失活。与先前的报道相反，发现在存在4mM Ca2+的情况下会发生快速激活/失活。钼酸根离子会减慢激活和失活，但不会阻止热激活。热激活/失活的复合物在大小上与未激活和Ca2+失活的复合物都不同。这一发现表明热诱导和Ca2+诱导的失活遵循不同的机制。
