• 我要登录|
  • 免费注册
    |
  • 我的丁香通
    • 企业机构:
    • 成为企业机构
    • 个人用户:
    • 个人中心
  • 移动端
    移动端
丁香通 logo丁香实验_LOGO
搜实验

    大家都在搜

      大家都在搜

        0 人通过求购买到了急需的产品
        免费发布求购
        发布求购
        点赞
        收藏
        wx-share
        分享

        Producing a Recombinant Flavin-Containing Monooxygenase from Coffea arabica in Escherichia coli for Screening of Potential Natural Substrates

        互联网

        537
        Only few biological functions have been related with flavin-containing monooxygenases (FMOs) in plants, such as specific roles in auxin biosynthesis, pathogen defense, and metabolism of glucosinolates. Biochemical characterization using recombinant proteins is a promising approach to determine the precise specificity of plant FMOs for potential natural substrates. FMOs may be very difficult to express in a soluble form due to their highly hydrophobic nature and this can be improved by fusing them to solubility-enhancing proteins, such as maltose-binding protein (MBP) and N-utilization substance A (NusA). Here we describe the expression of a recombinant FMO from Coffea arabica as a maltose-binding protein fusion in Escherichia coli and its purification by affinity chromatography, producing a ready-to-use protein for enzymatic activity assays.
        ad image
        提问
        扫一扫
        丁香实验小程序二维码
        实验小助手
        丁香实验公众号二维码
        扫码领资料
        反馈
        TOP
        打开小程序