Purification of riboflavin synthase by affinity chromatography.

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  • アフィニティクロマトグラフィーによるリボフラビンシンターゼの精製
  • アフィニティ クロマトグラフィー ニ ヨル リボフラビンシンターゼ ノ セイセ

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Abstract

Affinity chromatography with commercial AH-Sepharose 4B and an inhibitor as the ligand was used to purify riboflavin synthase. AH-Sepharose 4B was coupled with 6-carboxyethyl-7-hydroxy-8-ribityllumazine (an inhibitor of the enzyme reaction). The enzyme showed a specific affinity with the gel and could be eluted with 5mM 6, 7-dimethy-8-ribityl lumazine (the substrate) in 0.1M K2HPO4. The enzyme was purified 100-fold by chromatography, when the crude extract from Eremothecium ashbyii was used as the enzyme source. The specific activity (14, 600) of the purified enzyme indicates that the method can be used for purification of the enzyme.

Journal

  • Nippon Nōgeikagaku Kaishi

    Nippon Nōgeikagaku Kaishi 62 (7), 1077-1079, 1988

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

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