Purification and Properties of Aminopeptidase C from Chicken Skeletal Muscle(Food & Nutrition)
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概要
- 論文の詳細を見る
Aminopeptidase C was purified from fresh chicken skeletal muscle by ammonium sulfate fractionation, and by successive chromatography on DEAE-cellulose, Ultrogel AcA 34, DEAE-cellulose again, and an alanine AH-Sepharose 4B affinity column twice. The purified enzyme migrated as a single band by SDS-PAGE. Aminopeptidase C was purified about 300-fold over the crude extract with a yield of 0.6%. The molecular weight of this enzyme was found to be 185,000 by gel filtration in a Sepharose 6B column and 92,000 by SDS-PAGE. The optimum pH for the hydrolysis of L-leucine β-naphthylamide was 6.0-7.0, the enzyme being stable in the range of pH 6.5-8.0. The activity of this enzyme was strongly inhibited by EDTA and puromycin, and was high against the β-naphthylamide derivatives of Lys, Leu, Ala and Met. The enzyme was more active towards tri- and tetrapeptides than towards dipeptides.
- 社団法人日本農芸化学会の論文
- 1991-07-23
著者
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Kato Hiromichi
Department of Agricultural Chemistry, The University of Tokyo
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Kato H
Univ. Tokyo Tokyo Jpn
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Kato H
Department Of' Agricultural Chemistry The University Of Tokyo
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Kato Hiromichi
Department Of Agricultural Chemistry The University Of Tokyo
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Nishimura Toshihide
Department Of' Agricultural Chemistry The University Of Tokyo
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Nishimura Toshihide
Department Of Agricultural Chemistry The University Of Tokyo
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OKITANI Akihiro
Department of Animal Products Science and Technology, Nippon Veterinary and Zootechnical College
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Okitani A
Faculty Of Veterinary And Animal Science Nippon Veterinary And Animal Science University
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KATO Yutaka
Research Institute, Soda Aromatic Co., Ltd.
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Kato Yutaka
Research Institute Soda Aromatic Co. Ltd.
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OKITANI Akihiro
Department of Agricultural Chemistry, Faculty of Agriculture, The University of Tokyo
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