还原态台湾眼镜蛇心脏毒素的复性
Renaturation of a reduced Taiwan cobra cardiotoxin.
作者信息
Wong C H, Chen Y H, Hung M C, Wang K T, Ho C L, Lo T B
出版信息
Biochim Biophys Acta. 1978 Mar 28;533(1):105-11. doi: 10.1016/0005-2795(78)90553-6.
Refolding of a denatured protein obtained by reducing cardiotoxin from the Taiwan cobra with mercaptoethanol has been carried out in aqueous and non-aqueous solutions. Oxidation of the reduced protein in 0.05 M phosphate buffer (pH 7.2) resulted in isolating an active protein which showed, as compared to native cardiotoxin, identical conformation and biological activities such as lethality, antigenicity and muscle contracture inducing activity. On the other hand, the reduced protein was undergoing incorrect SS-pairing and several inactive products were formed in a mixture of 1,2-ethanediol and 1-propanol (1 : 1; v/v).
通过用巯基乙醇还原台湾眼镜蛇的心脏毒素而获得的变性蛋白质，已在水溶液和非水溶液中进行了重折叠。在0.05 M磷酸盐缓冲液（pH 7.2）中对还原后的蛋白质进行氧化，得到了一种活性蛋白质，与天然心脏毒素相比，该活性蛋白质具有相同的构象和生物学活性，如致死性、抗原性和诱导肌肉挛缩的活性。另一方面，在1,2 - 乙二醇和1 - 丙醇的混合物（1:1；v/v）中，还原后的蛋白质发生了不正确的二硫键配对，并形成了几种无活性的产物。
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