Monteil H, Rossel G, Boulouis D
Biochim Biophys Acta. 1975 Apr 8;382(4):465-78. doi: 10.1016/0005-2736(75)90215-1.
The Mg2+ -dependent ATPase (EC 3.6.I.3) of Proteus L-form membrane has been solubilized according to various procedures (Tris - HCL shock-wash with or without MG2+, EDTA, Triton X-100). The best results were obtained by the same 33mM Tris-HCL (pH 7.5) shock-wash without MG2+ used for ATPase of protoplasts from Streptococcus faecalis. The solubilized enzyme after 105 000 times g centrifugation was purified on acrylamide/agarose. The molecular weight was established to be 360 000 by gel filtration and by sedimentation coefficient (12.5 S). Polyacrylamide disc-gel electrophoresis in sodium dodecylsulphate revealed two classes or subunit of mol. wt. 64 000 (alpha) and 58 000 (beta), associated in ratio 1:1. We propose a formula alpha-3beta-3 for the native ATPase of Proteus L-forms. Structural similarities to ATPase of various origins are discussed.
变形杆菌L型细胞膜的Mg2+依赖性ATP酶（EC 3.6.I.3）已按照各种程序进行了增溶处理（用含或不含Mg2+、EDTA、Triton X-100的Tris - HCL进行冲击洗涤）。使用与粪链球菌原生质体ATP酶相同的不含Mg2+的33mM Tris-HCL（pH 7.5）冲击洗涤，获得了最佳结果。经105 000倍重力离心后的增溶酶在丙烯酰胺/琼脂糖上进行纯化。通过凝胶过滤和沉降系数（12.5 S）确定分子量为360 000。十二烷基硫酸钠聚丙烯酰胺圆盘凝胶电泳显示有两类分子量分别为64 000（α）和58 000（β）的亚基，其比例为1:1。我们提出变形杆菌L型天然ATP酶的分子式为α-3β-3。文中还讨论了与各种来源的ATP酶的结构相似性。
