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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.
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