The role of charge microheterogeneity of human myelin basic protein in the formation of phosphatidylglycerol multilayers |
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| Authors: | G W Brady D B Fein D D Wood M A Moscarello |
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| Institution: | 1. Center for Laboratories and Research New York State Department of Health Albany, New York 12201 USA;2. Department of Physics, Rensselaer Polytechnic Institute Troy, New York 12181 USA;3. Research Institute, The Hospital for Sick Children 555 University Avenue, Toronto, Ont., Canada M5G 1X8;1. Institute of Physiology and Pathophysiology, University of Heidelberg, D-69120 Heidelberg, Germany;2. Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, 05508-000, São Paulo, Brazil;3. Interdisciplinary Center for Neurosciences, University of Heidelberg, D-69120 Heidelberg, Germany;1. Division of General Academic Pediatrics, Department of Pediatrics, Massachusetts General Hospital, Boston, Massachusetts;2. Division of Pediatric Gastroenterology, Hepatology, and Nutrition, Department of Pediatrics, Columbia University Medical Center, New York City, New York;3. Department of Nutrition, Harvard T. H. Chan School of Public Health, Boston, Massachusetts;4. Department of Obstetrics and Gynecology, Massachusetts General Hospital, Boston, Massachusetts;5. Kraft Center for Community Health Leadership, Partners Healthcare, Boston, Massachusetts;1. Norwich Medical School, University of East Anglia, Norwich, UK;2. Division of Women''s Health, St Thomas'' Campus, King''s College London, UK;3. Elsie Bertram Diabetes Centre, Norfolk and Norwich University Hospital, Norwich, UK;4. Clinical Audit and Registries Management Service (CARMS), NHS Digital, Leeds, UK;5. National Diabetes Audit, NHS Digital, Leeds, UK;6. Maternal and Fetal Health Research Centre, St Mary''s Hospital, Manchester, UK;7. Department of Obstetrics, Singleton Hospital, Swansea Bay University Health Board, Swansea, UK;8. Princess Anne Hospital, University Hospital Southampton NHS Foundation Trust, Southampton, UK;9. NHS England and NHS Improvement, London, UK;10. Department of Diabetes and Endocrinology, St Mary''s Hospital, Imperial College Healthcare NHS Trust, London, UK;11. Division of Diabetes, Endocrinology and Metabolism, Imperial College London, London, UK;12. Division of Clinical and Population Sciences, Leeds Institute of Cardiovascular and Metabolic Medicine, University of Leeds, Leeds, UK;13. Department of Diabetes and Endocrinology, Northumbria Healthcare NHS Foundation Trust, Northumberland, UK;1. Department of Psychiatry, Xijing Hospital, Fourth Military Medical University, Xi''an, 710032, China;2. Department of Toxicology, Shaanxi Key Lab of Free Radical Biology and Medicine, The Ministry of Education Key Lab of Hazard Assessment and Control in Special Operational Environment, School of Public Health, Fourth Military Medical University, Xi’an, 710032, China;3. Institute of Neuroscience, Fourth Military Medical University, Xi''an, 710032, China;4. Department of Pediatrics, Xijing Hospital, Fourth Military Medical University, Xi''an, 710032, China;5. Department of Human Anatomy and Histology and Embryology, Basic Medical College, Ningxia Medical University, 750004, China;6. State Key Laboratory of Cancer Biology, Department of Pathology, Xijing Hospital and School of Basic Medicine, Fourth Military Medical University, Xi''an, 710032, China;1. Department of Psychiatry, Columbia University, 1051 Riverside Drive, New York, NY 10032, USA;2. Division of Molecular Imaging & Neuropathology, New York State Psychiatric Institute, 1051 Riverside Drive, Unit 42, New York, NY 10032, USA;3. Department of Biostatistics, Columbia University, 722 West 168th St., New York, NY 10032, USA;4. Nathan S. Kline Institute for Psychiatric Research, 140 Old Orangeburg Road, Orangeburg, NY 10962, USA;5. Department of Radiology, Columbia University, 622 West 168th St, New York, NY, USA;1. Liver Research Center, Division of Gastroenterology, Department of Medicine, Brown University, Providence, RI, USA;2. Departments of Neurology, Neurosurgery, and Pathology, Brown University, Providence, RI, USA;3. Rhode Island Hospital, The Alpert Medical School of Brown University, Providence, RI, USA;4. Neuroscience Graduate Program, Brown University, Providence, RI, USA |
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| Abstract: | Human myelin basic protein (HBP) was fractionated into its various charge isomers by chromatography on CM-52 columns at pH 10.6. Components 1,2,3 and "8" (C-1, C-2, C-3, and C-"8") were cleanly separated. Each component was combined with phosphatidylglycerol (PG) vesicles, at neutral pH at a concentration of 30% (w/w), protein/lipid. C-1, the most cationic of the components was the most effective at inducing the formation of multilayers when studied by liquid X-ray diffraction. C-3, which differs from C-1 by 2 positive charges was less effective than C-2. C-"8" was totally ineffective since the scattering pattern with this component was no different from that of the pure lipid. Thus a seemingly small change in net charge of the protein had a dramatic effect on the ability of the protein to organize the lipid into a crystalline, multilayer arrangement characteristic of compact myelin. |
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