牛肝硫醇-蛋白质二硫键氧化还原酶。蛋白质二硫键异构酶和谷胱甘肽-胰岛素转氢酶差异纯化及分离的另一种方法。
Bovine liver thiol-protein disulphide oxidoreductases. An alternative method for differential purification and resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase.
作者信息
Hillson D A, Freedman R B
出版信息
Biochem J. 1980 Nov 1;191(2):389-93. doi: 10.1042/bj1910389.
Abstract
- Protein disulphide-isomerase (EC 5.3.4.1) and glutathione-insulin transhydrogenase (EC 1.8.4.2) activities in bovine liver were studied in parallel during purification of 'thiol-protein disulphide oxidoreductase' by the procedure of Carmichael, Morin & Dixon [(1977) J Biol. Chem. 252, 7163-7167]. The two activities showed no quantitative co-purification and were partially resolved by (NH4)SO4 precipitation, indicating that distinct enzymes are present. 2. Protein disulphide-isomerase was purified by a relatively rapid method involving a combination of the early stages of the Carmichael procedure and covalent chromatography, with a new stepwise elution procedure. Ion-exchange chromatography yields a homogeneous preparation of mol.wt. 57 000. 3. The relationship between protein disulphide-isomerase, glutathione-insulin transhydrogenase and 'thiol-protein disulphide oxidoreductase' is discussed.
摘要
- 采用Carmichael、Morin和Dixon [(1977) J Biol. Chem. 252, 7163 - 7167]的方法对“硫醇-蛋白质二硫键氧化还原酶”进行纯化时，同时研究了牛肝中蛋白质二硫键异构酶（EC 5.3.4.1）和谷胱甘肽-胰岛素转氢酶（EC 1.8.4.2）的活性。这两种活性未呈现定量共纯化，且通过硫酸铵沉淀可部分分离，表明存在不同的酶。2. 蛋白质二硫键异构酶通过一种相对快速的方法进行纯化，该方法结合了Carmichael方法的早期阶段和共价层析，并采用新的分步洗脱程序。离子交换层析得到分子量为57000的均一制剂。3. 讨论了蛋白质二硫键异构酶、谷胱甘肽-胰岛素转氢酶和“硫醇-蛋白质二硫键氧化还原酶”之间的关系。
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引用本文的文献
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本文引用的文献
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2
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FEBS Lett. 1973 Dec 1;37(2):238-40. doi: 10.1016/0014-5793(73)80468-5.
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Biochim Biophys Acta. 1974 Dec 18;371(2):577-81.
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Metabolism of insulin and glucagon. Glutathione-insulin transhydrogenase from microsomes of rat liver.胰岛素与胰高血糖素的代谢。大鼠肝脏微粒体中的谷胱甘肽 - 胰岛素转氢酶。
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