Purification of some physicochemical properties of phenol oxidase from the larvae of house fly musca domestica vicina
Yamaura, I.; Yonekura, M.; Katsura, Y.; Ishiguro, M.; Funatsu, M.
Agricultural and Biological Chemistry 44(1): 55-60
1980
ISSN/ISBN: 0002-1369 Accession: 006233645
Phenoloxidase was purified from the larvae of housefly, M. 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 MW of phenoloxidase was 3.4 .times. 105 by Archibald's method and 3.1 .times. 105 by polyacrylamide gel disc electrophoresis. the isoelectric point of phenoloxidase was 4.7 by ampholine electrophoresis. The maximum and minimum absorptions were 280 nm and 251 nm, respectively, with purified phenoloxidase.