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  1. 080 繊維学部
  2. 0801 学術論文

Purification and characterization of UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase, with broad substrate specificity from tobacco cultured cells

http://hdl.handle.net/10091/10111
http://hdl.handle.net/10091/10111
e35b0c63-0900-41b0-a55f-d66da91e5c43
名前 / ファイル ライセンス アクション
Plant Plant Sci 2000.pdf (1.3 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2010-05-26
タイトル
言語 en
タイトル Purification and characterization of UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase, with broad substrate specificity from tobacco cultured cells
言語
言語 eng
キーワード
主題Scheme Other
主題 Nicotiana tabacum L. cv Bright Yellow
キーワード
主題Scheme Other
主題 glucosyltransferase
キーワード
主題Scheme Other
主題 scopoletin
キーワード
主題Scheme Other
主題 esculetin
キーワード
主題Scheme Other
主題 flavonoid
資源タイプ
資源 http://purl.org/coar/resource_type/c_6501
タイプ journal article
著者 Taguchi, G

× Taguchi, G

WEKO 41014

Taguchi, G

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Imura, H

× Imura, H

WEKO 41015

Imura, H

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Maeda, Y

× Maeda, Y

WEKO 41016

Maeda, Y

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Kodaira, R

× Kodaira, R

WEKO 41017

Kodaira, R

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Hayashida, N

× Hayashida, N

WEKO 41018

Hayashida, N

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Shimosaka, M

× Shimosaka, M

WEKO 41019

Shimosaka, M

Search repository
Okazaki, M

× Okazaki, M

WEKO 41020

Okazaki, M

Search repository
信州大学研究者総覧へのリンク
氏名 Taguchi, G
URL http://soar-rd.shinshu-u.ac.jp/profile/ja.uCDpjekV.html
信州大学研究者総覧へのリンク
氏名 Hayashida, N
URL http://soar-rd.shinshu-u.ac.jp/profile/ja.HVfmjekV.html
信州大学研究者総覧へのリンク
氏名 Shimosaka, M
URL http://soar-rd.shinshu-u.ac.jp/profile/ja.ZekmjekV.html
出版者
出版者 Elsevier
引用
内容記述タイプ Other
内容記述 Plant Science. 157(1):105-112 (2000)
書誌情報 Plant Science

巻 157, 号 1, p. 105-112, 発行日 2000
抄録
内容記述タイプ Abstract
内容記述 The enzyme UDP-glucose: hydroxycoumarin 7-O-glucosyltransferase (CGTase), which catalyzes the formation of scopolin from scopoletin, was purified approximately 1200-fold from a culture of 2,4-D-treated tobacco cells (Nicotiana tabacum L. cv. Bright Yellow T-13) with a yield of 7%. Purification to apparent homogeneity, as judged by SDS-PAGE, was achieved by sequential anion-exchange chromatography, hydroxyapatite chromatography, gel filtration, a second round of anion-exchange chromatography, and affinity chromatography on UDP-glucuronic acid agarose. The purified enzyme had a pH optimum of 7.5, an isoelectric point (pI) of 5.0, and a molecular mass of 49 kDa. The enzyme did not require metal cofactors for activity. Its activity was inhibited by Zn2+, Co2+ and Cu2+ ions, as well as by SH-blocking reagents. The K-m values for UDP-glucose, scopoletin and esculetin were 43, 150 and 25 mu M. respectively. A study of the initial rate of the reaction suggested that the reaction proceeded via a sequential mechanism. The purified enzyme preferred hydroxycoumarins as substrates but also exhibited significant activity with flavonoids. A database search using the amino terminus amino acid sequence of CGTase revealed strong homology to the amino acid sequences of other glucosyltransferases in plants.
資源タイプ(コンテンツの種類)
内容記述タイプ Other
内容記述 Article
ISSN
収録物識別子タイプ ISSN
収録物識別子 0168-9452
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA10531279
他の資源との関係:URI
識別子タイプ URI
関連識別子 http://www.elsevier.com/locate/plantsci
関連名称 http://www.elsevier.com/locate/plantsci
PubMed
識別子タイプ PMID
関連識別子 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?CMD=search&DB=pubmed&term=10940474
関連名称 10940474
DOI
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/S0168-9452(00)00270-3
関連名称 10.1016/S0168-9452(00)00270-3
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
WoS
表示名 Web of Science
URL http://gateway.isiknowledge.com/gateway/Gateway.cgi?&GWVersion=2&SrcAuth=ShinshuUniv&SrcApp=ShinshuUniv&DestLinkType=FullRecord&DestApp=WOS&KeyUT=000088553500011
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