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Phospholipid vesicle aggregation induced by human myelin basic protein

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Abstract

Human myelin basic protein isolated from the brains of individuals who died with multiple sclerosis was more potent in inducing the aggregation of egg phosphatidylcholine vesicles than was the basic protein isolated from the brains of normal individuals. The portion of myelin basic protein which bound to egg phosphatidylcholine vesicles was separated from the free protein by sucrose density gradient centrifugation. Similar amounts of basic protein from normal or from multiple sclerosis brains are bound to the lipid and no consistent differences in the NG, N′G dimethyl-arginine content of the protein fractions have been found.

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Authors and Affiliations

  1. Department of Biochemistry, McMaster University, L8N 3Z5, Hamilton, Ontario

    Sampath I. Sridhara & Richard M. Epand

  2. Research Institute, The Hospital for Sick Children, M5G 1X8, Toronto, Ontario

    Mario A. Moscarello

Authors
  1. Sampath I. Sridhara
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  2. Richard M. Epand
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  3. Mario A. Moscarello
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Sridhara, S.I., Epand, R.M. & Moscarello, M.A. Phospholipid vesicle aggregation induced by human myelin basic protein. Neurochem Res 9, 241–248 (1984). https://doi.org/10.1007/BF00964172

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