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通过在Triton X-100-琼脂糖中进行电泳从溶液中的蛋白质上去除未结合的十二烷基硫酸钠(SDS)。

Removal of unbound sodium dodecyl sulfate (SDS) from proteins in solution by electrophoresis through triton x-100-agarose.

作者信息

Lee L T, Deas J E, Howe C

出版信息

J Immunol Methods. 1978;19(1):69-75. doi: 10.1016/0022-1759(78)90009-1.

Abstract

Residual sodium dodecyl sulfate (SDS) introduces artifacts into immuno- and counterimmunoelectrophoretic analysis of proteins which have been eluted from preparative SDS-polyacrylamide gels. Unbound SDS can be removed by electrophoretic passage of eluted solutions through a barrier of Triton X-100 in agarose in which the anionic and non-ionic detergents interact to form micelles.

摘要

残留的十二烷基硫酸钠(SDS)会在对从制备型SDS聚丙烯酰胺凝胶上洗脱下来的蛋白质进行免疫电泳和对流免疫电泳分析时引入假象。未结合的SDS可通过将洗脱液电泳通过琼脂糖中Triton X-100的屏障来去除,其中阴离子和非离子洗涤剂相互作用形成胶束。

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