title: Covalent linkage of phosphoinositides to myelin basic protein: in vitro incorporation of [32P] phosphoinositides to myelin basic protein.
abstract: We have previously reported that the covalent attachment of phosphoinositides to myelin basic protein (MBP) occurs both in vivo and in vitro [Smith, R. A. et al. (1986) Biochemistry 25:2677-2681; Biochemistry 25:2682-2686; and Biochem. Biophys. Res. Comm. 316:426-432]. Phosphoinositidation of MBP was also detected when [32P] phosphoinositides were incubated with myelin pretreated with Triton X-100 and EGTA. Less than 10% of this covalent linkage of phosphoinositides to MBP survived after acidic treatment (0.1 N HCl at 37 degrees C for 10 min). MBP is predicted to lack sufficient hydrophobicity to bind to membranes as shown by analysis of its amino acid sequence for hydrophobic regions and thus its phosphoinositidation may provide an anchor for this purpose.
mesh_terms: D000255:Adenosine Triphosphate / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002851:Chromatography, High Pressure Liquid; D004533:Egtazic Acid / Q000494:pharmacology; D066298:In Vitro Techniques; D004676:Myelin Basic Protein / Q000378:metabolism*; D017830:Octoxynol; D010716:Phosphatidylinositols / Q000378:metabolism*; D011092:Polyethylene Glycols / Q000494:pharmacology
chemical_list: D004676:Myelin Basic Protein; D010716:Phosphatidylinositols; D011092:Polyethylene Glycols; D004533:Egtazic Acid; D000255:Adenosine Triphosphate; D017830:Octoxynol