A novel fragmentation of human myelin basic protein: identification of phosphorylated domains |
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| Authors: | K F Chan M A Moscarello G L Stoner H F Webster |
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| Institution: | 1. Laboratory of Experimental Neuropathology, NINCDS, NIH, Bethesda, MD 20892 USA;2. The Hospital for Sick Children, 555 University Ave., Toronto, Ontario, Canada;1. School of Food Science and Biotechnology, Food Safety Key Laboratory of Zhejiang Province, Zhejiang Gongshang University, Hangzhou 310018, China;2. College of Animal Science, Zhejiang University, Hangzhou 310058, China;1. Department of Education, Santa Clara University, 500 El Camino Real, Santa Clara, CA 95053, USA;2. Department of Education Studies, University of Oregon, Eugene, USA;1. Department of Emergency Medicine, University of North Carolina, Chapel Hill, NC;2. Department of Anesthesiology, University of North Carolina, Chapel Hill, NC;3. Department of Family Medicine, University of North Carolina, Chapel Hill, NC;4. Department of Emergency Medicine, St Joseph Mercy Hospital, Ypsilanti, MI;5. Department of Emergency Medicine, William Beaumont Hospital, Royal Oak, MI;6. Department of Emergency Medicine, University of Florida Health, Jacksonville, FL;7. Department of Emergency Medicine, Massachusetts General Hospital, Boston, MA;8. Department of Emergency Medicine, Baystate Medical Center, Springfield, MA;9. Spectrum Health, Grand Rapids, MI;10. Department of Emergency Medicine, North Shore Hospital System, Manhasset, NY;11. Department of Psychology and Neuroscience, Duke University, Durham, NC |
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| Abstract: | Human myelin basic protein (MBP) was fragmented into three major polypeptides comprised of a NH2-terminal domain (residues 1-83), a middle domain (residues 84-119) which contains an experimental allergic encephalitogenic determinant and a highly conserved triproline sequence, and a COOH-terminal domain (residues 120-170) by Staphylococcus aureus V8 protease at pH 4.0. These three polypeptides could be identified and purified by reversed-phase high-performance liquid chromatography. Analysis of the sites of phosphorylation of the component 1 of human MBP, the most cationic species, catalyzed by a purified Ca2+-activated and phospholipid-dependent protein kinase and cAMP-dependent protein kinase revealed that although these protein kinases could incorporate approximately 6 and 4 mol 32P, respectively, into MBP, none of the potential sites were located within the middle domain. |
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