Johnson E R, Oh K J, Wetlaufer D B
J Biol Chem. 1976 May 25;251(10):3154-7.
Regeneration of enzymic activity from reduced hen egg lysozyme peptide 1-127 was effected with a glutathione oxidation-reduction buffer. The rate of regeneration was nearly as great for peptide 1-127 as for reduced lysozyme itself, and the yields were the same (greater than 80%). The regenerated fragment 1-127 was shown to be indistinguishable from fragment 1-127 before reduction by ion exchange chromatography, amino acid analysis, polyacrylamide gel electrophoresis, and disulfide analysis. These results show that the COOH-terminal dipeptide Arg-Leu is not essential for the acquisition of the native three-dimensional structure of lysozyme.
用谷胱甘肽氧化还原缓冲液实现了还原型鸡蛋溶菌酶肽1 - 127酶活性的再生。肽1 - 127的再生速率与还原型溶菌酶本身几乎一样高,且产率相同(大于80%)。通过离子交换色谱、氨基酸分析、聚丙烯酰胺凝胶电泳和二硫键分析表明,再生的片段1 - 127与还原前的片段1 - 127无法区分。这些结果表明,COOH末端二肽Arg - Leu对于溶菌酶天然三维结构的获得并非必不可少。