Almiş-Kanigür G, Kan B, Kospançali S, Bermek E
FEBS Lett. 1982 Aug 16;145(1):143-6. doi: 10.1016/0014-5793(82)81223-4.
An inhibitor of protein synthesis was activated under high oxygen partial pressure (pO2) in hemin-supplemented and glutathione disulfide-free lysates from rabbit reticulocytes. This inhibitor shared some common features with other translational inhibitors from rabbit reticulocytes; that is, hemin-controlled repressor, glutathione disulfide-activated inhibitor and high pressure-activated inhibitor. It caused biphasic kinetics of inhibition which could be potentiated by ATP. Its activation was prevented by cAMP or glucose 6-phosphate. The high pO2-inhibitor could be partially purified from post-ribosomal supernatant containing ribosomal salt wash by precipitation between 0-50% (NH4)2SO4-saturation, Sephadex G-100, and DEAE-cellulose chromatography.
在来自兔网织红细胞的添加血红素且无谷胱甘肽二硫化物的裂解物中,一种蛋白质合成抑制剂在高氧分压(pO₂)下被激活。这种抑制剂与兔网织红细胞的其他翻译抑制剂有一些共同特征;即血红素控制的阻遏物、谷胱甘肽二硫化物激活的抑制剂和高压激活的抑制剂。它引起双相抑制动力学,ATP可增强这种抑制作用。cAMP或6-磷酸葡萄糖可阻止其激活。高pO₂抑制剂可通过在0 - 50%(NH₄)₂SO₄饱和度之间沉淀、Sephadex G - 100和DEAE - 纤维素色谱法从含有核糖体盐洗的核糖体后上清液中部分纯化。