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Phenoloxidase was purified from the larvae of housefly, Musca domestica vicina Maquart, by a procedure involving ammonium sulfate precipitation, extensive dialysis against deionized water, hydroxylapatite column chromatography and Sephadex G-200 gel filtration. Purified phenoloxidase was homogeneous on polyacrylamide gel disc electrophoresis and ultracentrifugation. The sedimentation coefficient of phenoloxidase was 13.5 S. The molecular weight of phenoloxidase was 3.4×105 by Archibald's method and 3.1×105 by polyacrylamide gel disc electrophoresis. The isoelectric point of phenoloxidase was 4.7 by ampholine electrophoresis. The maximum and minimum absorptions were found at 280 nm and 251 nm, respectively, with purified phenoloxidase.

Purification and some physico-chemical properties of phenoloxidase from the larvae of housefly.