Presence of multiple protein kinase activities in Coprinus macrorhizus |
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| Affiliation: | 1. Key Laboratory of Microbial Resources Collection and Preservation, Ministry of Agriculture, and Institute of Agricultural Resources and Regional Planning, Chinese Academy of Agricultural Sciences, Beijing 100081, China;2. Beijing Academy of Science and Technology, Beijing 100089, China;3. School of Environmental Sciences, University of Guelph, Guelph, Ontario N1G 2W1, Canada;1. Technology R&D Center, Hubei Tobacco (Group) Co., Ltd., Wuhan 430040, China;2. School of Life Science and Technology, Huazhong University of Science and Technology, Wuhan 430074, China;3. Department of Plant Pathology and Microbiology, Texas A&M University, College Station, TX 77843, USA;4. College of Resources and Environment, Gansu Agricultural University, Lanzhou 730030, China;1. Department of Plant Biology and Pathology, Rutgers, The State University of New Jersey, New Brunswick, NJ, 08901, USA;2. College of Forestry, Northwest A&F University, Yangling, Shaanxi, 712100, PR China;1. Marine College, Shandong University (Weihai), Weihai, 264209, China;2. Weihai fishery Technology Popularizing Station, Weihai, 264200, China;1. School of Biological Science and Technology, Liupanshui Normal University, Liupanshui, China;2. College of Mathematical Sciences, Harbin Engineering University, Harbin, China |
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| Abstract: | Protein kinase (ATP:protein phosphotransferase, EC 2.7.1.37) activity was found in crude extracts from monokaryotic mycelia of a basidiomycete, Coprinus macrorhizus. The enzyme activity of crude extracts was significantly inhibited by the addition of cyclic AMP and was influenced by the culture age of mycelia.Sepharose 6B chromatography resolved the protein kinase activity into four peaks designated as Peak I, II, III and IV. The activity of Peak II was stimulated in vitro by cyclic AMP, and that of Peaks I and III was inhibited by cyclic AMP. The activity of Peak IV was independent of cyclic AMP. The pH optima of these enzymes were found to be 6.5–7.0. The activities of these enzymes were promoted by Mg2+ and Mn2+, and were partially inhibited by Cu2+ and Zn2+. |
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