从大鼠肝脏100000g上清液中对两种石胆酸结合蛋白进行部分纯化。
Partial purification of two lithocholic acid-binding proteins from rat liver 100 000g supernatants.
作者信息
Strange R C, Cramb R, Hayes J D, Percy-Robb I W
出版信息
Biochem J. 1977 Sep 1;165(3):425-9. doi: 10.1042/bj1650425.
Abstract
- The partial purification of two lithocholic acid-binding proteins from liver 100 000g supernatants is described. 2. Gel-filtration, (NH4)2SO4 fractionation, Ca3(PO4)2 fractionation and ion-exchange chromatography were used. 3. Both proteins exhibited glutathione S-transferase activity; one may be the non-specific anion-binding protein ligandin. 4. Glutathione S-transferase activity of one of the binding proteins was inhibited by lithocholic acid.
摘要
- 本文描述了从肝脏100 000g上清液中对两种石胆酸结合蛋白进行部分纯化的过程。2. 使用了凝胶过滤、硫酸铵分级分离、磷酸钙分级分离和离子交换色谱法。3. 两种蛋白均表现出谷胱甘肽S-转移酶活性；其中一种可能是非特异性阴离子结合蛋白配体蛋白。4. 其中一种结合蛋白的谷胱甘肽S-转移酶活性被石胆酸抑制。
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Ligandin: a hepatic protein which binds steroids, bilirubin, carcinogens and a number of exogenous organic anions.配体蛋白：一种肝脏蛋白质，可结合类固醇、胆红素、致癌物及多种外源性有机阴离子。
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The identity of glutathione S-transferase B with ligandin, a major binding protein of liver.谷胱甘肽S-转移酶B与肝脏主要结合蛋白——配体蛋白的同一性。
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Equilibrium-dialysis studies of the interaction between cholic acid and 100000g-supernatant preparations from the rat liver.胆酸与大鼠肝脏100000g上清液制剂相互作用的平衡透析研究。
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10
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