title: Amphilphilic nature of spiralin, the major protein of the Spiroplasma citri cell membrane.
abstract: 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.
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis*; D055598:Chemical Phenomena; D002621:Chemistry; D003902:Detergents; D008565:Membrane Proteins / Q000032:analysis*; D012995:Solubility; D013149:Spiroplasma / Q000032:analysis*
chemical_list: D001426:Bacterial Proteins; D003902:Detergents; D008565:Membrane Proteins