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Primary Structure and Carbohydrate Binding Specificity of a Potent Anti-HIV Lectin Isolated from the Filamentous Cyanobacterium Oscillatoria agardhii

https://hiroshima.repo.nii.ac.jp/records/2007234
https://hiroshima.repo.nii.ac.jp/records/2007234
631afe52-e064-47cd-a099-7c4399641bba
名前 / ファイル ライセンス アクション
JBC_282_11021.pdf JBC_282_11021.pdf (1.6 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Primary Structure and Carbohydrate Binding Specificity of a Potent Anti-HIV Lectin Isolated from the Filamentous Cyanobacterium Oscillatoria agardhii
言語 en
作成者 Sato, Yuichiro

× Sato, Yuichiro

en Sato, Yuichiro

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Okuyama, Satomi

× Okuyama, Satomi

en Okuyama, Satomi

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Hori, Kanji

× Hori, Kanji

en Hori, Kanji

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アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利情報
権利情報 Copyright (c) 2007 by the American Society for Biochemistry and Molecular Biology.
主題
主題Scheme NDC
主題 470
内容記述
内容記述 The primary structure of a lectin,designated OAA, isolated from thefreshwater cyanobacterium, Oscillatoriaagardhii NIES-204, was determined by thecombination of Edman degradation andESI-mass spectrometry. OAA is apolypeptide (MW 13,925) consisting of twotandem repeats. Interestingly, each repeatsequence of OAA showed a high degree ofsimilarity to those of a myxobacterium,Myxococcus xanthus hemagglutinin(MBHA), and a marine red alga Eucheumaserra lectin (ESA-2). A systematic bindingassay with pyridylaminated oligosaccharidesrevealed that OAA exclusively binds to highmannose (HM) type N-glycans, but not toother N-glycans, including complex types,hybrid types and the pentasaccharide core,or oligosaccharides from glycolipids. OAAdid not interact with any of free mono-andoligomannoses that are constituents of thebranched oligomannosides. These resultssuggest that the core disaccharide, GlcNAc-GlcNAc, is also essential for binding to OAA.The binding activity of OAA to HMtype N-glycanswas dramatically decreased whenα1-2 Man was attached to α1-3 Manbranched from the α1-6 Man of thepentasaccharide core. This specificity ofOAA for HM type oligosaccharides isdistinct from other HM-binding lectins.Kinetic analysis with an HMheptasaccharide revealed that OAApossesses two carbohydrate-binding sitesper molecule, with an association constant of2.41×10^8M^-1. Furthermore, OAA potentlyinhibits HIV replication in MT-4 cells(EC50=44.5 nM). Thus, we have found anovel lectin family sharing similar structureand carbohydrate binding specificity amongbacteria, cyanobacteria, and marine algae.
言語 en
出版者
出版者 The American Society for Biochemistry and Molecular Biology
言語
言語 eng
資源タイプ
資源タイプ識別子 http://purl.org/coar/resource_type/c_6501
資源タイプ journal article
出版タイプ
出版タイプ AO
出版タイプResource http://purl.org/coar/version/c_b1a7d7d4d402bcce
関連情報
識別子タイプ DOI
関連識別子 10.1074/jbc.M701252200
関連情報
識別子タイプ DOI
関連識別子 http://dx.doi.org/10.1074/jbc.M701252200
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0021-9258
収録物識別子
収録物識別子タイプ NCID
収録物識別子 AA00251083
開始ページ
開始ページ 11021
書誌情報 Journal of Biological Chemistry
Journal of Biological Chemistry

巻 282, 号 15, p. 11021-11029, 発行日 2007-04-13
旧ID 21539
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