Abstract
Myelin basic protein and phosphatidylinositol-4-phosphate are phosphorylated in vitro by ATP and solubilized rat brain myelin. When both substrates are present together, the rate of phosphorylation of each is increased about eight-fold. It appears likely that the phosphate turnover of myelin basic protein and of phosphatidylinositol-4-phosphate are coupled in vivo.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Culture Media
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Histones / metabolism
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In Vitro Techniques
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Male
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Myelin Basic Protein / metabolism*
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Myelin Sheath / metabolism*
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Phosphatidylinositol Phosphates*
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Phosphatidylinositols / metabolism*
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Phospholipids / metabolism
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Phosphorylation
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Protein Kinases / metabolism
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Rats
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Solubility
Substances
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Culture Media
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Histones
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Myelin Basic Protein
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Phosphatidylinositol Phosphates
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Phosphatidylinositols
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Phospholipids
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phosphatidylinositol 4-phosphate
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Protein Kinases