Horbach M E, Sies H, Akerboom T P
Institut für Physiologische Chemie I, Heinrich-Heine-Universität Düsseldorf, Germany.
Eur J Biochem. 1994 May 15;222(1):91-6. doi: 10.1111/j.1432-1033.1994.tb18845.x.
Glutathione transferases purified from plasma membrane and microsomal fractions from rat liver share similar enzymic properties. The activity of both proteins with 1-chloro-2,4-dinitrobenzene can be stimulated about 10-15-fold by N-ethylmaleimide. No activation is observed using p-nitrobenzylchloride as a substrate. The enzymes are immunologically related as indicated by Western-blot analysis using antibodies against the microsomal glutathione transferase or against a synthetic peptide corresponding to the amino acid positions 55-64 of microsomal glutathione transferase. Isolated plasma membrane and microsomal glutathione transferases possess the same amino-terminal amino acid sequence and digestion with different proteases results in identical fragment patterns as displayed by SDS/PAGE. These data suggest that plasma membrane and microsomal glutathione transferase are identical proteins.
从大鼠肝脏的质膜和微粒体组分中纯化得到的谷胱甘肽转移酶具有相似的酶学特性。这两种蛋白质与1-氯-2,4-二硝基苯的活性可被N-乙基马来酰亚胺刺激约10-15倍。以对硝基苄基氯为底物时未观察到激活作用。如使用抗微粒体谷胱甘肽转移酶的抗体或针对与微粒体谷胱甘肽转移酶氨基酸位置55-64对应的合成肽进行蛋白质免疫印迹分析所示，这些酶在免疫上相关。分离得到的质膜和微粒体谷胱甘肽转移酶具有相同的氨基末端氨基酸序列，用不同蛋白酶消化后，SDS/PAGE显示出相同的片段模式。这些数据表明质膜和微粒体谷胱甘肽转移酶是相同的蛋白质。
