Purification and Characterization of Cyclic AMP-Binding Protein from Ganoderma lucidum |
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Authors: | WANG Qi KIM Jung-Sik CHUNG Ki-Chul |
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Institution: | 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 |
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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 . |
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Keywords: | cAMP-binding protein Purification Characterization Ganoderma lucidum |
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