Purification and Characterization of Porcine Skeletal Muscle Aminopeptidase T, a Novel Metallopeptidase Homologous to Leukotriene A4 Hydrolase

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概要

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• A novel aminopeptidase, Aminopeptidase T (APase T), was purified from porcine skeletal muscle following successive column chromatography: twice on DEAE-cellulose, hydroxyapatite, and Sephacryl S-200 HR using Leu-β-naphthylamide (LeuNap) as a substrate. The molecular mass of the enzyme was 69 kDa on SDS–PAGE. The optimum pH towards LeuNap of the enzyme was about 7. The enzyme activity was strongly inhibited by bestatin and was negatively affected by ethylenediaminetetraacetic acid (EDTA). Chlorine-activated APase T liberated Leu, Ala, Met, Pro, and Arg from Nap derivatives. The APase T gene consisted of an ORF of 1,836 bp encoding a protein of 611 amino acid residues. The APase T was highly homologous to bovine, human, and mouse Leukotriene A4 hydrolase (LTA4H), a bifunctional enzyme which exhibits APase and epoxide hydrolase activity.

著者

• NISHIMURA Toshihide

  Faculty of Applied Biological Science, Hiroshima University

• Iefuji Haruyuki

  Graduate School of Biosphere Science, Hiroshima University

• SARKER Mohammed

  Graduate School of Biosphere Science, Hiroshima University

• MATSUDA Shinji

  Graduate School of Biosphere Science, Hiroshima University

• MIZUTANI Osamu

  National Research Institute of Brewing

• RAO Shengbin

  Graduate School of Biosphere Science, Hiroshima University

• MIGITA Koshiro

  Faculty of Food Science and Technology, Nippon Veterinary and Life Science University

• GOTO-YAMAMOTO Nami

  Graduate School of Biosphere Science, Hiroshima University

• Nishimura Toshihide

  Faculty Of Applied Biological Science Hiroshima University

• Iefuji Haruyuki

  Graduate School Of Biosphere Sci. Hiroshima Univ.

• Mizutani Osamu

  National Res. Inst. Of Brewing

• Matsuda Shinji

  Graduate School Of Biosphere Science Hiroshima University

• Rao Shengbin

  Graduate School Of Biosphere Science Hiroshima University

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