Identification of an apyrase activating protein and of calmodulin in Solanum tuberosum |
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| Affiliation: | 1. Division of Pharmacoengineering and Molecular Pharmaceutics, and Center for Nanotechnology in Drug Delivery, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA;2. David H. Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, Cambridge, MA 02139, USA;3. Key Laboratory of Functional Polymer Materials, Ministry of Education, Institute of Polymer Chemistry, College of Chemistry, State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin 300071, China;1. State Key Laboratory of Automotive Dynamic Simulation and Control, Jilin University, Changchun, 130022, China;2. China Automotive Engineering Research Institute Co., Ltd, Chongqin, 401122, China |
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| Abstract: | Three types of effector proteins have been isolated from a partially purified protein preparation of potato tuber. One of the proteins is a typical calmodulin which has no effect on apyrase. The two other proteins modulate ATPase and ADPase activities; one of them with an activating and the other with an inhibitory effect on apyrase. Calmodulin from potato tuber purified to homogeneity had a Mr of 17 500 and an isoelectric point of 4.4. Although the apyrase activating protein is not a pure fraction it differs from calmodulin because unlike this protein it is independent of calcium and does not activate cyclic nucleotide phosphodiesterase from bovine heart. Treatment of the activating protein with tetranitromethane reduces its effect on apyrase, while no change was detected upon treatment with bisdithionitrobenzoic acid. |
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