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  1. 農学部
  2. 学術雑誌掲載論文 (農学部)

Zebrafish tyrosylprotein sulfotransferase: Molecular cloning, expression, and functional characterization

http://hdl.handle.net/10458/1872
http://hdl.handle.net/10458/1872
ad6199de-564c-404f-b52f-78a950afb5c2
名前 / ファイル ライセンス アクション
bcb82.pdf bcb82.pdf (2.1 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2009-02-26
タイトル
タイトル Zebrafish tyrosylprotein sulfotransferase: Molecular cloning, expression, and functional characterization
言語 en
言語
言語 eng
キーワード
言語 en
主題Scheme Other
キーワード Molecular cloning, Tyrosylprotein sulfotransferase, Zebra fish
資源タイプ
資源タイプ journal article
著者 Mishiro, Emi

× Mishiro, Emi

WEKO 3139

en Mishiro, Emi

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Liu, Ming-Yih

× Liu, Ming-Yih

WEKO 3140

en Liu, Ming-Yih

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Sakakibara, Yoichi

× Sakakibara, Yoichi

WEKO 2805
e-Rad 90295197

en Sakakibara, Yoichi

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Suiko, Masahito

× Suiko, Masahito

WEKO 2643
e-Rad 00128357

en Suiko, Masahito

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Liu, Ming-Cheh

× Liu, Ming-Cheh

WEKO 2650

en Liu, Ming-Cheh

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抄録
内容記述タイプ Abstract
内容記述 By employing the reverse transcriptase - polymerase chain reaction technique in conjunction with 3′ rapid amplification of cDNA ends, a full-length cDNA encoding a zebrafish (Danio rerio) tyrosylprotein sulfotransferase (TPST) was cloned and sequenced. Sequence analysis revealed that this zebrafish TPST is, at the amino acid sequence level, 66% and 60% identical to the human and mouse TPST-1 and TPST-2, respectively. The recombinant form of the zebrafish TPST, expressed in COS-7 cells, exhibited a pH optimum at 5.75. Manganese appeared to exert a stimulatory effect on the zebrafish TPST. The activity of the enzyme determined in the presence of 20 mM MnCl2 was more than 2.5 times that determined in the absence of MnCl2. Of the other nine divalent metal cations tested at a 10 mM concentration, Co2+ also showed a considerable stimulatory effect, while Ca2+, Pb2+, and Cd2+ exerted some inhibitory effects. The other four divalent cations, Fe2+, Cu 2+, Zn2+, and Hg2+, inhibited completely the sulfating activity of the zebrafish TPST. Using the wild-type and mutated P-selectin glycoprotein ligand-1 N-terminal peptides as substrates, the zebrafish TPST was shown to exhibit a high degree of substrate specificity for the tyrosine residue on the C-terminal side of the peptide. These results constitute a first study on the cloning, expression, and characterization of a zebrafish cytosolic TPST.
言語 en
書誌情報 en : Biochemistry and cell biology
en : Biochimie et biologie cellulaire

巻 82, 号 2, p. 295-303, 発行日 2004-04
出版者
出版者 National Research Council Canada
言語 en
ISSN
収録物識別子タイプ ISSN
収録物識別子 08298211
書誌レコードID
収録物識別子タイプ NCID
収録物識別子 AA10506067
著者版フラグ
出版タイプ VoR
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