Coliphage Derived Sialidase Preferentially Recognizes Nonreducing End of Polysialic Acid(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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概要

• 論文の詳細を見る

• Bacteriophages infecting Escherichia coli K1 strains generally have endotype polysialic acid-degrading enzymes. We studied the digestion mechanism of a sialidase associated with the coliphage 63D using polysialic acid radiolabeled at its nonreducing end or reducing end. It was found that this enzyme preferentially recognizes the nonreducing end of polysialic acid, suggesting that the 63D associated sialidase does not randomly digest its substrate but acts like an exotype glycosidase.

• 社団法人日本生物工学会の論文
• 2006-02-25

著者

• 三宅 克英

  名大院・工・生物機能

• IIJIMA SHINJI

  Department of Chemical Engineering, Faculty of Engineering, Nagoya University

• Iijima S

  Department Of Biotechnology Graduate School Of Engineering Nagoya University

• Iijima Shinji

  Department Of Biotechnology School Of Engineering Naogya University

• Iijima Shinji

  Department Of Biotechnology Faculty Of Engineering Nagoya University

• Iijima S

  Department Of Biotechnology Faculty Of Engineering Nagoya University

• Iijima Shinji

  Department Of Chemical Engineering Nagoya University

• Murai K

  Osaka Univ. Osaka Jpn

• Koike Y

  Nagoya Univ. Nagoya Jpn

• KATAOKA YOHEI

  Department of Biotechnology Graduate School of Engineering, Nagoya University

• Koike Yoichi

  Department Of Biotechnology Graduate School Of Engineering Nagoya University

• MIYAKE Katsuhide

  Ecotopia Science Institute, Nagoya University

• Miyake K

  Nagoya University

• Miyake Katsuhide

  Ecotopia Institute Nagoya University

• 三宅 克英

  名大院・工・化学生物工

• 三宅 克英

  Department Of Biotechnology Graduate School Of Engineering Nagoya University

• Iijima Shinji

  Department of Biotechnology, Graduate School of Engineering, Nagoya University

• IIJIMA Shinji

  Department of Agricultural Chemistry, The University of Tokyo

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