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Two epitopes responsible for the catalytic activity of heme oxygenase‐1 identified by phage display

机译:通过噬菌体展示鉴定出负责血红素加氧酶-1催化活性的两个表位

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Heme oxygenase‐1 (HO‐1) catalyzes the oxidative degradation of heme. The catalytic mechanism of the HO‐1 reaction has been determined gradually by studies of its crystal structure and HO‐1 mutants. However, the neutralizing epitopes responsible for HO‐1 activity remain elusive. Screening of a phage display library revealed four epitopes that could interact with the polyclonal antibody prepared by immunizing rabbits with the purified HO‐1 protein. Two of these four epitopes are responsible for HO‐1 catalytic activity because their antibodies were able to neutralize HO‐1 activity. The results of the present study shed further light on the molecular character of HO‐1.
机译:血红素加氧酶-1(HO-1)催化血红素的氧化降解。 HO-1反应的催化机理已通过研究其晶体结构和HO-1突变体逐渐确定。但是,负责HO-1活性的中和表位仍然难以捉摸。噬菌体展示文库的筛选揭示了四个表位,这些表位可能与通过用纯化的HO-1蛋白免疫兔而制备的多克隆抗体相互作用。这四个表位中的两个负责HO-1催化活性,因为它们的抗体能够中和HO-1活性。本研究的结果进一步揭示了HO-1的分子特征。

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