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首页> 外文期刊>The Biochemical Journal >An altered T2 beta translocase of the glucose-6-phosphatase system in the membrane of the endoplasmic reticulum from livers of Ehrlich-ascites-tumour-bearing mice.
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An altered T2 beta translocase of the glucose-6-phosphatase system in the membrane of the endoplasmic reticulum from livers of Ehrlich-ascites-tumour-bearing mice.

机译:Ehrlich-腹水-荷瘤小鼠肝脏内质网膜中葡萄糖-6-磷酸酶系统的T2β移位酶改变。

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摘要

The inhibitory interactions of orthophosphate (P1) with the glucose-6-phosphatase system of intact microsomes derived from the livers of normal and Ehrlich-ascites-tumour-bearing mice reveal the appearance of a novel form of the T2 beta translocase component of the glucose-6-phosphatase system in tumour-stressed mice. Kinetic studies, with and without 20 mM P1, show a strictly classical competitive inhibition, with a K1,P1 of 4.2 mM, with disrupted microsomes from both control and tumour-bearing mouse liver. Inhibition was also observed with intact microsomes from livers of control mice, and contributions by both competitive and non-competitive components of inhibition were quantified by calculation of Kis,P1 and Kii,P1 values respectively. However, little inhibition was noted with intact microsomes from the livers of tumour-bearing mice. It is concluded that this novel form of T2 beta is less able to transport Pi, from the cytosol to the endoplasmic reticulum lumen, perhaps because of the tumour-related increased Km for Pi transport in this direction.
机译:正磷酸盐(P1)与正常小鼠和艾氏腹水肿瘤小鼠肝脏中完整微粒体的葡萄糖-6-磷酸酶系统的抑制性相互作用揭示了葡萄糖的T2β转位酶组分的新型形式肿瘤应激小鼠中的-6-磷酸酶系统。有和没有20 mM P1的动力学研究表明,严格的经典竞争抑制作用,K1,P1为4.2 mM,且来自对照小鼠和荷瘤小鼠肝脏的微粒体均被破坏。还观察到了来自对照小鼠肝脏的完整微粒体的抑制作用,并且分别通过计算Kis,P1和Kii,P1值来量化竞争性和非竞争性抑制作用的贡献。然而,来自荷瘤小鼠肝脏的完整微粒体几乎没有抑制作用。结论是,这种新形式的T2β不能将Pi从胞质转运到内质网腔,这可能是由于与肿瘤相关的Km在该方向上的转运。

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