ω-エポキシアルキルα-グルコシドによるグリコシダーゼの親和標識 Affinity Labelling of Glycosidase by ω-Epoxyalkyl α-Glucoside

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著者

    • 木村 淳夫 KIMURA Atsuo
    • 北海道大学大学院農学研究科応用生命科学専攻 Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University
    • 奥 忠武 OKU Tadatake
    • 日本大学生物資源科学部農芸化学科 Department of Agriculture, College of Bioresource Sciences, Nihon University
    • サン サン マー MAR San San
    • 北海道大学大学院農学研究科応用生命科学専攻 Division of Apploed Bioscience, Graduate School of Agriculture, Hokkaido University
    • 千葉 誠哉 CHIBA Seiya
    • 北海道大学大学院農学研究科応用生命科学専攻 Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University

抄録

The suicide substrate of isomalto-dextranase was designed, and the ω-epoxyalkyl α-glucosides, of which the alkyl carbons were three to six, were synthesized. The 2', 3'-epoxypropyl α-glucoside did not decrease the activity. ω-Epoxyalkyl α-glucosides with four to six alkyl carbons resulted in inactivation which followed the pseudo-first order kinetics. A detailed kinetic analysis on inactivation was done, and the results obtained supported that the compounds were suicide substrates for isomalto-dextranase. All ω-epoxyalkyl α-glucosides synthesized inactivated β-amylase. The C<SUB>5</SUB>-al-kyl compound was the most effective for the inactivation of isomalto-dextranase, but β-amylase was strongly inactivated by the C<SUB>4</SUB>-alkyl compound. The discrimination of inhibitors by the two en-zymes was considered to be based on the difference in their substrate recognition, in which β-amy-lase recognizes the maltosyl residue and isomalto-dextranase recognizes the isomaltosyl residue having one methylene group longer than the maltosyl residue. No inactivation for α-amylase was observed with the ω-epoxyalkyl α-glucosides. The 3', 4' epoxybutyl α-glucoside did not show any effect on the substrate binding. Conduritol B epoxide, a suicide substrate for α-glucosidase, also caused no inactivation or no inhibition of α-amylase activity. These findings were applied to the α-amylase assay in the enzyme mixture coexistent with β-amylase and α-glucosidase. Since 3', 4' ep-oxybutyl α-glucoside was hydrolyzed by α-glucosidase, a mixture of three enzymes was incubated with conduritol B epoxide at first, and then treated with 3', 4'-epoxybutyl α-glucoside, resulting in the complete inactivation of α-glucosidase and β-amylase. This procedure was shown to be useful in the determination of α-amylase in preparations containing α-glucosidase and β-amylase.

収録刊行物

  • 応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience

    応用糖質科学 : oyo toshitsu kagaku = Journal of applied glycoscience 47(2), 235-241, 2000-06-30

    The Japanese Society of Applied Glycoscience

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各種コード

  • NII論文ID(NAID)
    10008251915
  • NII書誌ID(NCID)
    AN10453916
  • 本文言語コード
    JPN
  • 資料種別
    REV
  • ISSN
    13403494
  • NDL 記事登録ID
    5436139
  • NDL 雑誌分類
    ZP24(科学技術--化学・化学工業--糖・澱粉)
  • NDL 請求記号
    Z17-15
  • データ提供元
    CJP書誌  NDL  J-STAGE 
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