Preparative slab electrofocusing of methane monooxygenase from a type I methanotroph Methylomonas GYJ3.
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.
Liu
A M
AM
Lanzhou Institute of Chemical Physics, Chinese Academy of Sciences.
Li
S B
SB
Yu
W L
WL
Zhang
F
F
Chen
J X
JX
Su
P
P
D007525:Isoelectric Focusing / Q000379:methods; D007700:Kinetics; D008772:Methylococcaceae / Q000201:enzymology*; D010105:Oxygenases / Q000302:isolation & purification* / Q000378:metabolism
D010105:Oxygenases; C021555:methane monooxygenase