Purification and Properties of Aminopeptidase H from Porcine Skeletal Muscle(Biological Chemistry)
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概要
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Aminopeptidase H was purified from fresh porcine muscle by ammonium sulfate fractionation and successive chromatographies of DEAE-cellulose, Ultrogel AcA 34, Phenyl-Sepharose CL-4B, hydroxylapatite, and a second DEAE-cellulose. The purified enzyme migrated as a single band on SDS-PAGE. Aminopeptidase H has activity against both L-leucine β-naphthylamide (LeuNap) and α-N-benzoyl-DL-arginine β-naphthylamide (BzArgNap). The molecular weight of the purified enzyme was 51,000 on SDS-PAGE and 390,000 on an Ultrogel AcA 34 column chromatography. The optimum pH for the hydrolysis of LeuNap and BzArgNap was 8.0. The Km values for the hydrolysis of LeuNap and BzArgNap were 0.37 and 1.25mM, respectively. These activities were strongly inhibited by monoiodoacetic acid and leupeptin, but not affected by EDTA, phenylmethylsulfonyl fluoride, pepstatin, or bestatin. The enzyme had the large activities against Met-, Leu-, Lys-, Ala-, Glu-, and SerNap and no activity against ProNap.
- 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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Rhue Mee
Department Of Agricultural Chemistry The University Oj Tokyo
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Rhyu Mee
Department Of Agricultural Chemistry Faculty Of Agriculture 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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