Micrococcus lysodeikticus ATPase: Purification by preparative gel electrophoresis and subunit structure studied by urea and sodium dodecylsulfate gel electrophoresis

Micrococcus lysodeikticus ATPase was purified by preparative gel electrophoresis after its “shock wash” release from the membrane. The method afforded the highest yield of pure protein in the minimum time as compared with former purification procedures. The pure protein had a specific activity of 7 μmol P_i·min^?1·mg^?1 with incubation times not longer than 3 min, 345 000 mol. wt and was not stimulated by trypsin. By gel electrophoresis at alkaline pH (8.5) in 8 M urea or in sodium dodecylsulfate, the ATPase revealed a complex pattern with two major subunits (α and β) and two minor ones (γ and δ). The non-identity between the major subunits was demonstrated.