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Isolation of a novel variant of secretory component with low affinity to dimeric immunoglobulin a by immobilised metal ion affinity chromatography
http://hdl.handle.net/10241/00012972
http://hdl.handle.net/10241/000129725932a26a-05b8-4be0-ac54-503e0a8d43e6
Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2022-07-16 | |||||
タイトル | ||||||
タイトル | Isolation of a novel variant of secretory component with low affinity to dimeric immunoglobulin a by immobilised metal ion affinity chromatography | |||||
タイトル | ||||||
タイトル | Isolation of a novel variant of secretory component with low affinity to dimeric immunoglobulin a by immobilised metal ion affinity chromatography | |||||
言語 | en | |||||
言語 | ||||||
言語 | eng | |||||
著者 |
山田, 潔
× 山田, 潔× Mizukoshi, Nobutaka× Kawata, Aya× Ono, Megumi× Hizono, Terumasa× 橋本, 啓× 東, 徳洋× Yamada, Kiyoshi× Mizukoshi, Nobutaka× Kawata, Aya× Ono, Megumi× Hizono, Terumasa× Hashimoto, Kei× Azuma, Norihiro |
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書誌情報 |
International Dairy Journal en : International Dairy Journal 巻 122, p. 105103, 発行日 2021-07-16 |
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関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://www.sciencedirect.com/science/article/pii/S095869462100131X | |||||
関連名称 | Elsevier Publisher Edition | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | https://www.sciencedirect.com/science/article/am/pii/S095869462100131X | |||||
関連名称 | Best available version URL | |||||
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 | |||||
アクセス権 | ||||||
アクセス権 | metadata only access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | By applying immobilised metal affinity chromatography to a free secretory component (FSC) preparation from bovine milk, we identified a novel FSC variant with lower affinity to dimeric immunoglobulin A. Using cDNA analysis, we found a novel His to Arg mutation at the 81st residue where the amino acid is well conserved among species. The IgA-binding portion of polymeric immunoglobulin receptor (pIgR) consists of five Ig-like domains (D1–D5); the first complementarity-determining region (CDR1) of D1 is especially critical to the noncovalent binding of pIgR to IgA. The mutation at position 81 occurred within D1, but at the beginning of the E/F loop on the opposite side of CDRl; this region is located at the interface with D2. Given that residues in D2 may form hydrogen bonds with D1, the mutation to Arg may have caused a positive charge that disturbed hydrogen bonding, altered domain relative orientation, and thereby lowered affinity. | |||||
出版者 | ||||||
出版者 | Elsevier | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 09586946 | |||||
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内容記述タイプ | Other | |||||
内容記述 | text | |||||
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出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 | |||||
WEKOアイテムタイプ | ||||||
内容記述タイプ | Other | |||||
内容記述 | 学術雑誌論文 / Journal Article |