肝阴离子结合蛋白在溴磺酞钠结合中的作用。
Role of hepatic anion-binding protein in bromsulphthalein conjugation.
作者信息
Kaplowitz N, Percy-Robb I W, Javitt N B
出版信息
J Exp Med. 1973 Aug 1;138(2):483-7. doi: 10.1084/jem.138.2.483.
Abstract
Using gel filtration, the binding of both glutathione and Bromsulphthalein (BSP) to a liver-soluble protein was found to be identical. BSP-conjugating activity (glutathione S-aryltransferase) was present only in the fractions corresponding to the two protein-bound markers. Using a highly sensitive assay, with 3,4-dichloronitrobenzene, the pattern of glutathione S-aryltransferase activity was found to coincide with Y protein. This evidence suggests that Y protein, or ligandin, has a dual role in hepatic transport: a specific enzymic function in the conjugation of certain anions with glutathione in addition to a transport function in the intracellular binding of organic anions.
摘要
利用凝胶过滤法发现，谷胱甘肽和溴磺酞（BSP）与一种肝可溶性蛋白的结合情况相同。BSP结合活性（谷胱甘肽S-芳基转移酶）仅存在于与两种蛋白结合标志物相对应的组分中。使用一种高度灵敏的检测方法，即利用3,4-二氯硝基苯，发现谷胱甘肽S-芳基转移酶活性模式与Y蛋白相符。这一证据表明，Y蛋白或配体蛋白在肝脏转运中具有双重作用：除了在细胞内结合有机阴离子方面具有转运功能外，在某些阴离子与谷胱甘肽结合过程中还具有特定的酶功能。
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本文引用的文献
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THE IMPORTANCE OF CONJUGATION WITH GLUTATHIONE FOR SULFOBROMOPHTHALEIN SODIUM (BSP) TRANSFER FROM BLOOD TO BILE.谷胱甘肽结合对磺溴酞钠（BSP）从血液向胆汁转运的重要性。
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The intrahepatic conjugation of sulfobromophthalein and glutathione in the dog.狗体内磺溴酞钠与谷胱甘肽的肝内共轭作用。
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A liver enzyme that conjugates sulfobromophthalein sodium with glutathione.一种能使磺溴酞钠与谷胱甘肽结合的肝脏酶。
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