Purification of component A of the soluble methane monooxygenase of Methylococcus capsulatus (Bath) by high-pressure gel permeation chromatography.

A major improvement in the purification of the oxygenase protein (component A) of the methane monooxygenase has been effected. By employing high-pressure gel permeation chromatography several purification steps may be omitted from the previously published scheme. Furthermore the yield of the protein is enhanced and more importantly the recovered protein displays an increased specific activity, unlike that purified by other techniques.