A coat protein from bacteriophage fd: I. Hydrodynamic measurements and biological characterization |
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| Affiliation: | 1. Bioenergy Research Centre, Department of Bioinformatics & Biotechnology, Government College University Faisalabad, Faisalabad 38000, Pakistan;2. Department of Chemical Engineering, Al-Balqa’a Applied University, Amman, Jordan;3. College of Bioengineering, Sichuan University of Science and Engineering, Zigong 643000, People’s Republic of China;4. Department of Environmental Sciences & Engineering, Government College University Faisalabad, Faisalabad 38000, Pakistan;5. Institute of Advanced Technology, Universiti Putra Malaysia, 43400 UPM Serdang, Selangor, Malaysia;6. Chemistry Department, College of Science, King Saud University, Riyadh 1145, Saudi Arabia;7. Soil Salinity Research Institute, Pindi Bhattian, Pakistan;8. UR Physico-Chimie des Materiaux Solides, Chemistry Department, Science College, Tunis El Manar University, 2092 Tunis, Tunisia;1. Department of Civil Engineering, Federal University of Viçosa, Av. Peter Henry Rolfs, s/n, Campus da Universidade Federal de Viçosa, Viçosa3, Minas Gerais 36570-900, Brazil;2. Department of Soil Science, Federal University of Viçosa, Av. Peter Henry Rolfs, s/n, Campus da Universidade Federal de Viçosa, Viçosa, Minas Gerais 36570-900, Brazil;3. Department of Water Resources and Sanitation, Federal University of Lavras, Campus Universitario, Lavras, Minas Gerais, 37200-000, Brazil;1. College of Marine Equipment and Mechanical Engineering, Jimei University, Xiamen 361021, China;2. College of Ocean and Earth Sciences, Xiamen University, Xiamen 361102, China;3. Fujian Key Laboratory of Coastal Pollution Prevention and Control, Key Laboratory of the Ministry of Education for Coastal and Wetland Ecosystems, College of the Environment & Ecology, Xiamen University, Xiamen 361102, China |
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| Abstract: | A coat protein has been isolated from highly purified fd bacteriophage disintegrated in phenol. Dissociation of the isolated protein to the monomeric state has only been achieved in 1% sodium dodecyl sulphate. At lower concentrations of the detergent as well as in several other solvents, the protein exists in the form of uniformly sized oligomers, probably heptamers or octamers. Protein dissolved in concentrated urea and dialysed versus neutral buffer aggregates to give rod-shaped particles with approximately the diameter of virus particles, but otherwise unlike virus in appearance. Such protein functions in blocking fd receptive sites of the bacterial host and in inactivating fd antiserum, although without complete exhaustion. The implications of these findings for the structure of the aggregated protein are discussed. |
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