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首页> 外文期刊>The Biochemical Journal >AN ALTERED T-2-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 T-2-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:EHRLICHS-ASTES-荷瘤小鼠肝脏内质网膜中葡萄糖-6-磷酸酶系统的T-2-BETA转座酶

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摘要

The inhibitory interactions of orthophosphate (P-i) 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 T-2 beta translocase component of the glucose-6-phosphatase system in tumour-stressed mice. Kinetic studies, with and without 20 mM P-i, show a strictly classical competitive inhibition, with a K-i,K-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 K-is,K-P1 and K-ii,K-Pi 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 T2B is less able to transport P-i, from the cytosol to the endoplasmic reticulum lumen, perhaps because of the tumour-related increased K-m for P-i transport in this direction.
机译:正磷酸盐(Pi)与正常和Ehrlich-腹水-肿瘤小鼠肝脏的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一种新型的T-2β转位酶组分的出现肿瘤应激小鼠体内的葡萄糖-6磷酸酶系统。在有和没有20 mM P-i的情况下进行的动力学研究表明,严格的经典竞争性抑制作用(K-i,K-P1为4.2 mM)受到了来自对照组和荷瘤小鼠肝脏的微粒体的破坏。还观察到了来自对照小鼠肝脏的完整微粒体的抑制作用,并且通过分别计算K-is,K-P1和K-ii,K-Pi值来量化竞争性和非竞争性抑制成分的贡献。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T2B不太可能将P-1从胞质转运到内质网腔,这可能是由于肿瘤相关的K-m在此方向上的转运。

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