Purification and Properties of Sweet Potato NADPH-Cytochrome c (P-450) Reductase
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概要
- 論文の詳細を見る
NADPH-cytochrome c reductase, strictly NADPH-cytochrome P-450 reductase, was purified by chromatography through DEAE-cellulose, 2',5'-ADP-Sepharose, and Sephadex G-100 columns after solubilization from microsomes from Ccratocystis fimbriatainfected sweet potato root tissue with Emulgen 913. The enzyme existed in three forms after solubilization which migrated to positions corresponding to molecular weights of 81,000, 75,000 and 72,000 on an SDS-polyacrylamide gel. Trypsin treatment of the enzyme species with the largest polypeptide yielded the species with the smallest one. After sucrose density gradient centrifugation of the pellet fraction obtained by centrifugation at 100,000 ×g of the crude extract, the enzyme species with the largest poly-peptide was present in the particulate fractions, whereas that with the smallest one was only found at the top of the gradient. We conclude that the enzyme species with the largest polypeptide is in an intact, amphipathic form, whereas that with the smallest one, and probably also the other species, is its hydrophilic domain produced by an endogenous protease(s). The K_m values of the enzyme in the intact form for NADPH and cytochrome c were 7.7 and 2.3 μM, respectively.
- 日本植物生理学会の論文
著者
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Asahi Tadashi
Laboratory of Biochemistry, School of Agriculture, Nagoya University
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Fujita Masayuki
Laboratory of Food Hygienics, Faculty of Agriculture, Kagawa University
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Asahi T
Fukui Prefectural Univ. Fukui Jpn
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Asahi Tadashi
Laboratory Of Biochemistry Faculty Of Agriculture Nagoya University
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Fujita Masayuki
Laboratory Of Biochemistry Faculty Of Agriculture Nagoya University:(present)laboratory Of Food Hygi
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Asahi Tadashi
Laboralory Of Biochemistry Faculty Of Agriculture Nagoya University
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