title: Preparative slab electrofocusing of methane monooxygenase from a type I methanotroph Methylomonas GYJ3.
abstract: The isolation and purification of methane monooxygenase from a type I methanotroph Methylomonas GYJ3 to near homogeneity is reported. The isoelectric focusing in flat-bed granulated gels has resolved the methane monooxygenase into three protein components. The specific activity of the enzyme is 198.4 n mol per min per mg protein, degree of purification 4.13-fold. Recovery of the focused proteins is high and elution simple. Several purification steps may be omitted from the previously published scheme by other techniques.
authors: Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences.
authors: A M
authors: AM
authors: Liu
authors: S B
authors: SB
authors: Li
authors: W L
authors: WL
authors: Yu
authors: F
authors: F
authors: Zhang
authors: J X
authors: JX
authors: Chen
authors: P
authors: P
authors: Su
mesh_terms: D007525:Isoelectric Focusing / Q000379:methods; D007700:Kinetics; D008772:Methylococcaceae / Q000201:enzymology*; D010105:Oxygenases / Q000302:isolation & purification* / Q000378:metabolism
chemical_list: D010105:Oxygenases; C021555:methane monooxygenase