Recognition of Receptor Lipopolysaccharides by Spike G Protein of Bacteriophage φX174

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概要

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• The spike G protein of bacteriophage φX174 was prepared as a hexa histidine-tagged G protein (HisG). In the enzyme-linked plate assay, HisG bound specifically to lipopolysaccharides (LPSs) of the φX174-sensitive strains, and did not bind to LPSs of the φX174-insensitive strains. The truncated G protein obtained after trypsin digestion of HisG had the similar affinity to the LPSs to HisG, indicating that eight amino acid residues from the N-terminus are not essential to the binding with the LPSs.

• 社団法人日本農芸化学会の論文
• 2000-09-23

著者

• Kato M

  Nagoya Univ. Aichi Jpn

• INAGAKI Minoru

  Department of Life Science, Faculty of Bioresources, Mie University

• KARITA Shuichi

  Center for Molecular Biology and Genetics Mie University

• Kato M

  Dep. Of Biological Mechanisms And Functions Graduate School Of Bioagricultural Sciences Nagoya Univ.

• KAWAURA Tomoko

  Department of Life Science, Faculty of Bioresources, Mie University

• KATO Muneharu

  Department of Life Science, Faculty of Bioresources, Mie University

• NISHIKAWA Shiro

  Department of Life Science, Faculty of Bioresources, Mie University

• KASHIMURA Naoki

  Department of Life Science, Faculty of Bioresources, Mie University

• Kawaura Tomoko

  Department Of Life Science Faculty Of Bioresources Mie University

• Karita S

  Graduate School Of Regional Innovation Studies Mie Univ.

• Inagaki Masao

  Department Of Life Science Faculty Of Bioresources Mie University

• Nishikawa Shiro

  Department Of Life Science Faculty Of Bioresources Mie University

• Kashimura N

  Department Of Life Science Faculty Of Bioresources Mie University

• Kashimura Naoki

  Department Of Bioscience Mie University

• Inagaki Minoru

  Department Of Life Science Faculty Of Bioresources Mie University

• Nishikawa Shiro

  Department of Bioscience, Faculty of Bioresources

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