Heat-stable enterotoxin (STh) of human enterotoxigenic Escherichia coli (strain SK-1). Structure-activity relationship.

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概要

• 論文の詳細を見る

• For examination of the structure-activity relationship of ST<SUB>h</SUB>, five shorter analogs of ST<SUB>h</SUB> lacking one to five N-terminal amino acid residues of ST<SUB>h</SUB> were synthesized. The synthetic peptides were confirmed to have the same intramolecular disulfide linkages as those in native ST<SUB>h</SUB>. These peptides caused fluid accumulation in the intestine of suckling mice at almost the same molar levels as that of native ST<SUB>h</SUB>. The toxicities of these peptides were also neutralized by antisera raised against native ST<SUB>h</SUB>. These results indicated that the toxic and antigenic sites of ST<SUB>h</SUB> are both located in the amino acid sequence between the Cys residue at the 5th position from the N-terminus and the C-terminal Tyr residue.

• 公益社団法人 日本化学会の論文

著者

• Shimonishi Yasutsugu

  Institute For Protein Research Osaka University

• Aimoto Saburo

  Institude For Protein Research Osaka University

• Hara Saburo

  Department Of Applied Biology Kyoto Institute Of Technology

• Watanabe Hiroyuki

  Institute Of Molecular And Cellular Biosciences University Of Tokyo

• Miwatani Toshio

  Research Institute For Microbial Diseases Osaka University

• Ikemura Haruo

  Institute for Protein Research, Osaka University

• Takeda Tae

  Research Institute for Microbial Diseases, Osaka University

• Takeda Yoshifumi

  Institute for Protein Research, Osaka University

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• Heat-stable enterotoxin (STh) of human enterotoxigenic Escherichia coli (strain SK-1). Structure-activity relationship.

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