Identification of the tryptophan residue located at the saccharide binding site of castor bean hemagglutinin.

DOI DOI オープンアクセス
  • ABSAR Nural
    Laboratory of Biochemistry, Faculty of-Agriculture, Kyushu University
  • YAMASAKI Nobuyuki
    Laboratory of Biochemistry, Faculty of-Agriculture, Kyushu University
  • FUNATSU Gunki
    Laboratory of Biochemistry, Faculty of-Agriculture, Kyushu University

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説明

The tryptophan residue present at the saccharide-binding site of castor bean hemagglutinin (CBH) was identified. A peptide containing a modified tryptophan residue was isolated from the tryptic digest of S-carboxymethylated B-chain obtained from an inactive derivative of CBH (2-Oxa-CBH), in which two tryptophan residues/mol were oxidized with N-bromosuccinimide, by gel filtration on a Sephadex G-50 followed by high performance liquid chromatography. Analytical data for the isolated peptide indicated that the tryptophan residue at position 131 on the B-chain was modified in 2-Oxa-CBH.<br> From these and earlier results, it is suggested that the tryptophan residue at 131 on each B-chain is closely associated with the saccharide-binding activity of CBH. The specific role of tryptophan residue at 131 in the saccharide-binding site of CBH is also discussed.

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詳細情報 詳細情報について

  • CRID
    1390282681440758912
  • NII論文ID
    110006322825
  • NII書誌ID
    AA00515312
  • DOI
    10.1271/bbb1961.50.3071
    10.1080/00021369.1986.10867884
  • COI
    1:CAS:528:DyaL2sXpvVarsA%3D%3D
  • ISSN
    18811280
    00021369
  • 本文言語コード
    en
  • データソース種別
    • JaLC
    • Crossref
    • CiNii Articles
    • OpenAIRE
  • 抄録ライセンスフラグ
    使用不可

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