通过谷胱甘肽亲和层析法纯化虹鳟肝脏谷胱甘肽S-转移酶会改变其等电行为。
The purification of the hepatic glutathione S-transferases of rainbow trout by glutathione affinity chromatography alters their isoelectric behaviour.
作者信息
Ramage P I, Nimmo I A
出版信息
Biochem J. 1983 May 1;211(2):523-6. doi: 10.1042/bj2110523.
Abstract
- The basic glutathione S-transferases from rainbow-trout liver were more stable than the acidic ones. 2. The apparent pI values of these enzymes were lowered when they were eluted from a glutathione affinity column by reduced glutathione at pH 8.85. 3. The pI effect was not a function of the high pH alone, was diminished under conditions less favourable to glutathione oxidation, and did not occur when S-hexylglutathione affinity chromatography was used instead.
摘要
- 虹鳟鱼肝中的碱性谷胱甘肽S-转移酶比酸性谷胱甘肽S-转移酶更稳定。2. 当这些酶在pH 8.85的条件下用还原型谷胱甘肽从谷胱甘肽亲和柱上洗脱时，其表观pI值会降低。3. pI效应并非仅由高pH引起，在不利于谷胱甘肽氧化的条件下会减弱，且当使用S-己基谷胱甘肽亲和色谱法时不会出现这种效应。
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