Partial purification of a nucleoside triphosphatase from the inner membrane of the chloroplast envelope of pea |
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| Authors: | D R McCarty B R Selman |
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| Institution: | 1. Division of Engineering and Applied Science, California Institute of Technology, Pasadena, CA 91125, USA;2. Univ. Grenoble Alpes, CNRS, Grenoble INP, 3SR, F-38000 Grenoble, France;1. Department of Atmospheric Sciences, School of Environmental Studies, China University of Geosciences, Wuhan, China;2. Center for Severe Weather and Climate and Hydro-geological Hazards, Wuhan, China;1. Department of Pathobiology, Faculty of Veterinary Medicine, Shahid Bahonar University of Kerman, Kerman, Iran;2. Molecular Microbiology Research Group, Shahid Bahonar University of Kerman, Kerman, Iran;3. Medical Mycology and Bacteriology Research Center, Kerman University of Medical Sciences, Kerman, Iran;4. Department of Microbiology (Bacteriology and Virology), Afzalipour Faculty of Medicine, Kerman University of Medical Sciences, Kerman, Iran;5. Infectious and Tropical Diseases Research Center, Hormozgan Health Institute, Hormozgan University of Medical Sciences, Bandar Abbas, Iran |
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| Abstract: | A Mg2+-NTPase has been partially purified from the inner membrane of the pea chloroplast envelope. Isolated envelope membranes were solubilized with Triton X-100 and fractionated by DEAE-Sephadex chromatography, followed by ultrafiltration and sucrose density gradient centrifugation. An approximate 35-fold increase in the specific activity of the vanadate and sodium fluoride sensitive NTPase was obtained. Analysis of the partially purified NTPase by sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed a single 37-kDa polypeptide that appeared to be associated with the activity. In support of this identification, it is demonstrated that the 37-kDa polypeptide can be photolabeled with 8-azido-ATP. |
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