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Isolation, Purification and Characterization of Glutamate Dehydrogenase from Porcine Brain

Tang JingTang Yunming

Key Laboratory of Eco-environments in Three Gorges Reservoir Region, Ministry of Education, Chongqing Sweet Potato Engineering Research Center, School of Life Science, Southwest University

摘要:To obtain pure glutamate dehydrogenase from porcine brain and explore its enzymological properties, the glutamate dehydrogenase which showed a single band on SDS-PAGE had been purified from porcine brain by frozen, homogenization, ammonium sulfate precipitation, DEAE-Sepharose chromatography and Superdex-200 chromatography. Its multiple of purification was 70.07 and its specific activity was13.63 U/mg. 24.61% of the glutamate dehydrogenase activity was recovered. The enzyme had a relative molecular mass of 330.08 KD. The relative molecular mass of the subunit was about 56.04 KD. The optimum temperature and pH of this enzyme were 55℃ and 8.2 respectively. The glutamate dehydrogenase displayed excellent stability at temperature below 40℃ and pH 6-8. Its apparent Km towards NADH was 0.084 mmol/L. The enzyme activity could be strongly inhibited when interacting with methanol, ethanol, isopropanol, SDS, oxalic acid, ascorbic acid, Cu2+, Co2+, or Zn2+ and activated when interacting with EDTA.
会议名称:

2019 1st International Biology and Medicine Conference(IBMC 2019)

会议时间:

2019-05-11

会议地点:

印度尼西亚雅加达

  • 专辑:

    基础科学

  • 专题:

    生物学

  • 分类号:

    Q55

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