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  1. 紀要
  2. お茶の水女子大學自然科學報告
  3. 50(1)

Multi-specificities of the N-Acetylglucosamine-Binding Lectin from Psathyrella velutina Mushroom toward Acidic Glycoconjugates

http://hdl.handle.net/10083/861
http://hdl.handle.net/10083/861
c41d9452-ece1-4292-9ab8-48f622f5779b
名前 / ファイル ライセンス アクション
KJ00004470905.pdf KJ00004470905.pdf (1.2 MB)
Item type 紀要論文 / Departmental Bulletin Paper(1)
公開日 2007-04-23
タイトル
タイトル Multi-specificities of the N-Acetylglucosamine-Binding Lectin from Psathyrella velutina Mushroom toward Acidic Glycoconjugates
言語
言語 eng
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ departmental bulletin paper
著者 Ueda, Haruko

× Ueda, Haruko

WEKO 70659

Ueda, Haruko

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Kojima, Kyoko

× Kojima, Kyoko

WEKO 70660

Kojima, Kyoko

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Saitoh, Takeshi

× Saitoh, Takeshi

WEKO 70661

Saitoh, Takeshi

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Ogawa, Haruko

× Ogawa, Haruko

WEKO 70662

Ogawa, Haruko

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著者(ヨミ)
識別子Scheme WEKO
識別子 70663
姓名 ウエダ, ハルコ
著者(ヨミ)
識別子Scheme WEKO
識別子 70664
姓名 コジマ, キョウコ
著者(ヨミ)
識別子Scheme WEKO
識別子 70665
姓名 サイトウ, タケシ
著者(ヨミ)
識別子Scheme WEKO
識別子 70666
姓名 オガワ, ハルコ
内容記述
内容記述タイプ Other
内容記述 A lectin from the fruiting body of Psathyrella velutina (PVL) has been reported to be specific for nonreducing terminal N-acetylglucosamine (GlcNAc) residue. PVL was found to exhibit multispecificity toward acidic glycoconjugates, i.e., polysaccharides, sialoglycoproteins, and sulfatide. PVL was purified by single-step affinity chromatography on an N-acetylchitooligosaccharides (GlcNAc_<5-6>)-Sepharose column. The binding specificities of PVL were studied using neoproteoglycans and neoglycoproteins involving heparin or GlcNAc_<5-6>. PVL was shown, by both membrane analysis and solid phase assay, to bind with heparin neoproteoglycans. The binding was inhibited by polygalacturonic acid, dextran sulfate, or fucoidan as well as heparin, but not by GlcNAc, other glycosaminoglycans, colominic acid, or DNA. The pH-dependencies of the binding to heparin and to GlcNAc_<5-6> were different. Biotinylation of PVL destroyed the heparin binding activity while retaining the GlcNAc binding activity. In addition, circular dichroism spectroscopy of PVL indicated that a small conformational change of PVL is induced by binding with GlcN\
Ac but not with heparin, suggesting that the binding sites for acidic polysaccharides and GlcNAc are independently located on PVL. On the other hand. PVL bound to sialoglycoproteins on solid phase assays, and the binding was inhibited with GlcNAc or desialylation treatment, indicating that PVL recognizes N-acetylneuraminic acid residue in glycoproteins at GlcNAc-binding site. The binding of PVL to sulfatide was not inhibited by GlcNAc, N-acetylneuraminic acid, or heparin. These findings indicate that the binding specificities of PVL to glycoconjugates are quite different from those reported for oligosaccharides and PVL is a novel member of muluspecific lectin in higher fungi.
書誌情報 お茶の水女子大學自然科學報告

巻 50, 号 1, p. 31-45, 発行日 1999-07-15
ISSN
収録物識別子タイプ ISSN
収録物識別子 00298190
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AN00033958
フォーマット
内容記述タイプ Other
内容記述 application/pdf
形態
1178164 bytes
日本十進分類法
主題Scheme NDC
主題 400
出版者
出版者 お茶の水女子大学
資源タイプ
内容記述タイプ Other
内容記述 紀要論文
資源タイプ・ローカル
紀要論文
資源タイプ・NII
Departmental Bulletin Paper
資源タイプ・DCMI
text
資源タイプ・ローカル表示コード
03
所属
Department of Advanced Biosciences, Graduate School of Humanities and Sciences, Ochanomizu University
所属
Department of Chemistry, Faculty of Science, Ochanomizu University
所属
The Mushroom Research Institute of Japan
所属
Department of Advanced Biosciences, Graduate School of Humanities and Sciences, Ochanomizu University
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