Wróblewski H
J Bacteriol. 1979 Nov;140(2):738-41. doi: 10.1128/jb.140.2.738-741.1979.
Spiralin could not be solubilized in the absence of detergents, and it was shown by charge-shift crossed immunoelectrophoresis that this protein was capable of binding detergents under nondenaturing conditions. These properties indicate the amphiphilic nature of spiralin, which therefore should be regarded as an intrinsic membrane protein. The efficiency of mild (ionic and neutral) detergents to solubilize spiralin was as follows: deoxycholate greater than lauroyl sarcosinate, cholate, taurocholate, taurodeoxycholate greater than Triton X-100 greater than Brij 58 greater than Tween 20, indicating that mild ionic detergents were more effective than neutral ones. Solubilization of spiralin was quantitative with sodium deoxycholate. It was also shown that although a membrane protein is not extractable by a given detergent from the membrane, this does not necessarily mean that the protein is not soluble in this detergent.
在没有去污剂的情况下，螺旋蛋白无法溶解，电荷转移交叉免疫电泳表明该蛋白在非变性条件下能够结合去污剂。这些特性表明螺旋蛋白具有两亲性，因此应被视为一种内在膜蛋白。温和（离子型和中性）去污剂溶解螺旋蛋白的效率如下：脱氧胆酸盐大于月桂酰肌氨酸钠、胆酸盐、牛磺胆酸盐、牛磺脱氧胆酸盐大于曲拉通X-100大于聚山梨醇酯58大于吐温20，这表明温和离子型去污剂比中性去污剂更有效。脱氧胆酸钠能定量溶解螺旋蛋白。还表明，尽管一种膜蛋白不能被某种特定去污剂从膜中提取出来，但这并不一定意味着该蛋白不溶于这种去污剂。
