Purification and Kinetic Properties of Phenoloxidase from Pupae of the Housefly(Biological Chemistry)
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概要
- 論文の詳細を見る
Phenoloxidase was purified from pupae of the housefly, Musca domestica L. The purification procedures included ammonium sulfate precipitation, affinity chromatography and Sephadex G-200 gel filtration. The final preparations appear to be homogeneous based on results obtained from polyacrylamide gel electrophoresis. The molecular weight of phenoloxidase was estimated to be 330,000, as determined by gel filtration. The kinetic properties of phenoloxidase were studied using six catecholamines as substrates. The preferred order of substrates for phenoloxidase was found to be N-β-alanyldopamine > dopamine > N-acetyldopamine > norepinephrine > epinephrine > DOPA.
- 社団法人日本農芸化学会の論文
- 1989-05-23
著者
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FUNATSU Masaru
Department of Applied Microbial Technology, The Kumamoto Institute of Technology
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Hara Tatsuru
Laboratory Of Biological Chemistry Faculty Of Agriculture Saga University
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Funatsu M
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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Funatsu Masaru
Department Of Applied Microbial Technology The Kumamoto Institute Of Technology
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TSUKAMOTO Takuji
Laboratory of Biological Chemistry, Faculty of Agriculture, Saga University
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MARUTA Kazunari
Laboratory of Biological Chemistry, Faculty of Agriculture, Saga University
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Hara Toshio
Laboratory Of Biological Chemistry Faculty Of Agriculture Saga University
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Tsukamoto T
Laboratory Of Biological Chemistry Faculty Of Agriculture Saga University
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Maruta Kazunari
Laboratory Of Biological Chemistry Faculty Of Agriculture Saga University
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