Solubilisation of methane monooxygenase from Methylococcus capsulatus (Bath).

摘要: The membrane-bound (particulate) form of methane monooxygenase from Methylococcus capsulatus (Bath) has been solubilised using the non-ionic detergent dodecyl-beta-D-maltoside. A wide variety detergents were tested and found to solubilise membrane proteins but did not yield in a that could be subsequently activated. After solubilisation with dodecyl-beta-D-maltoside, enzyme activity was recovered either egg or soya-bean lipids. Attempts further purify solubilized monooxygenaser protein into its component polypeptides unsuccessful resulted complete loss activity. major present had molecular masses 49 kDa, 23 kDa 22 which similar those seen crude extracts [Prior, S. D. & Dalton H. (1985) J. Gen. Microbiol. 131, 155-163]. Studies on substrate inhibitor specificities indicated membrane-associated forms quite each other differed substantially well-characterised soluble cells grown low copper regime synthesised independently particulate monooxygenase.