Structure-activity relationship of Escherichia coli heat-stable enterotoxin: Role of Ala residue at position 14 in toxin-receptor interaction.

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概要

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• A heat-stable enterotoxin (ST<SUB>h</SUB>) produced by a human strain of enterotoxigenic <I>Escherichia coli</I> consists of 19 amino residues including 6 half-cystine residues. Analogs of ST<SUB>h</SUB> from positions 6 to 19 with replacements of the Ala residue at position 14 by other amino acid residues were synthesized by a solid-phase method and examined by biological and biochemical methods. This Ala residue was demonstrated to be very important for expression of the toxicity of ST<SUB>h</SUB> and for interaction of the toxin with its receptor protein(s).

• 公益社団法人 日本化学会の論文

著者

• SUGIMURA Takashi

  Basic Research Laboratory, Himeji Institute of Technology

• TAI Akira

  Basic Research Laboratory, Himeji Institute of Technology

• SATO Takashi

  Institute for Materials Research, Tohoku University

• Shimonishi Yasutsugu

  Institute For Protein Research Osaka University

• Hidaka Yuji

  Institute For Protein Research Osaka University

• OZAKI Hiroshi

  Institute for Protein Research, Osaka University

• Takeda Yoshifumi

  Faculty Of Pharmaceutical Sciences Tokyo University Of Science (rikadai)

• Yamasaki Shinji

  Faculty of Medicine, Kyoto University

• Ito Hideaki

  Faculty of Medicine, Kyoto University

• Hirayama Toshiya

  The Institute of Medical Science, The University of Tokyo

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