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高等学校化学研究 ›› 2004, Vol. 20 ›› Issue (5): 588-593.

• Articles • 上一篇    下一篇

Purification and Characterization of Cyclic AMP-Binding Protein from Ganoderma lucidum

WANG Qi1, KIM Jung-Sik2, CHUNG Ki-Chul2   

  1. 1. College of Chinese Medicinal Materials, Jilin Agricultural University, Changchun 130118, P. R. China;
    2. Department of Genetic Engineering, College of Agriculture, Chonnam National University, Kwangju 500-757, Korea
  • 收稿日期:2003-12-09 出版日期:2004-10-24 发布日期:2011-08-06
  • 基金资助:

    Supported by Korea Science and Engineering Foundation(KOSEF).

Purification and Characterization of Cyclic AMP-Binding Protein from Ganoderma lucidum

WANG Qi1, KIM Jung-Sik2, CHUNG Ki-Chul2   

  1. 1. College of Chinese Medicinal Materials, Jilin Agricultural University, Changchun 130118, P. R. China;
    2. Department of Genetic Engineering, College of Agriculture, Chonnam National University, Kwangju 500-757, Korea
  • Received:2003-12-09 Online:2004-10-24 Published:2011-08-06
  • Supported by:

    Supported by Korea Science and Engineering Foundation(KOSEF).

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被引次数

7

摘要： Cyclic AMP-binding protein was purified 30 fold from the mycelia of Ganoderma lucidum by the methods of ammonium sulfate precipitation, DEAE-cellulose, phospho-cellulose ion exchange chromatography and Sephacryl S-100 gel filtration.The molecular mass of the purified protein is 34.5 kDa and 17 kDa by Sephacryl S-100 gel filtration and SDS-ployacrylamide gel electrophoresis, respectively.From these results it is suggested that the protein has a homometric dimmer structure.The pI of the purified protein is pH 8.2 by native isoelectric focusing gel.The half-life of the protein activity in 10% glycerol at 4 ℃ is 7 d in crude extract, but its half-life is only 3 d under purifying conditions.The optimal conditions of the protein activity are at 1 ℃ and pH 7.5.Its activity is increased 6 times by 1 mmol/L Zn2+ and is slightly inhibited by cGMP,Cu2+ and Mn2+.

关键词: cAMP-binding protein, Purification, Characterization, Ganoderma lucidum

Abstract: Cyclic AMP-binding protein was purified 30 fold from the mycelia of Ganoderma lucidum by the methods of ammonium sulfate precipitation, DEAE-cellulose, phospho-cellulose ion exchange chromatography and Sephacryl S-100 gel filtration.The molecular mass of the purified protein is 34.5 kDa and 17 kDa by Sephacryl S-100 gel filtration and SDS-ployacrylamide gel electrophoresis, respectively.From these results it is suggested that the protein has a homometric dimmer structure.The pI of the purified protein is pH 8.2 by native isoelectric focusing gel.The half-life of the protein activity in 10% glycerol at 4 ℃ is 7 d in crude extract, but its half-life is only 3 d under purifying conditions.The optimal conditions of the protein activity are at 1 ℃ and pH 7.5.Its activity is increased 6 times by 1 mmol/L Zn2+ and is slightly inhibited by cGMP,Cu2+ and Mn2+.

Key words: cAMP-binding protein, Purification, Characterization, Ganoderma lucidum