McGrew B R, Green D M
Department of Biochemistry, University of New Hampshire, Durham 03824.
Anal Biochem. 1990 Aug 15;189(1):68-74. doi: 10.1016/0003-2697(90)90045-b.
The inclusion of 1% casein or bovine serum albumin in buffer used to reactivate enzymes subjected to sodium dodecyl sulfate (SDS)-polyacrylamide electrophoresis resulted in accelerated removal of SDS and restoration of nuclease and beta-galactosidase enzyme activities. Nuclease and beta-galactosidase activities which are absent from gels after longer wash procedures are detectable with this technique. Enzyme activity in gels prepared with SDS which contained inhibitory contaminants was partially restored by the casein wash procedure. The threshold of detection of two-dimensionally separated deoxyribonuclease I using the casein wash procedure was 1 picogram.
在用于使经十二烷基硫酸钠（SDS）-聚丙烯酰胺凝胶电泳处理的酶重新激活的缓冲液中加入1%的酪蛋白或牛血清白蛋白，可加速SDS的去除，并恢复核酸酶和β-半乳糖苷酶的活性。经过较长时间洗涤程序后凝胶中缺失的核酸酶和β-半乳糖苷酶活性，用该技术可检测到。用含有抑制性污染物的SDS制备的凝胶中的酶活性，通过酪蛋白洗涤程序可部分恢复。使用酪蛋白洗涤程序二维分离的脱氧核糖核酸酶I的检测阈值为1皮克。
