title: Phosphorylation of myelin basic protein by glycogen phosphorylase kinase.
abstract: The ability of homogeneous glycogen phosphorylase kinase (Phk) from rabbit skeletal muscle to phosphorylate bovine brain myelin basic protein (MBP) was investigated. Phk could incorporate a maximum of 1.9 mol phosphate/mol MBP. The apparent Km and Vmax for Phk phosphorylation of MBP were 27 microM and 90 nmol/min per mg enzyme, respectively. Properties of MBP phosphorylation by Phk are similar to those of phosphorylase as a substrate. Only serine residues of MBP are phosphorylated by Phk. Phosphorylation sites of MBP by Phk are not identical to those by cAMP-dependent protein kinases.
mesh_terms: D000818:Animals; D002417:Cattle; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D004676:Myelin Basic Protein / Q000378:metabolism*; D010764:Phosphorylase Kinase / Q000378:metabolism*; D010763:Phosphorylase b / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D011817:Rabbits; D012694:Serine / Q000378:metabolism; D013997:Time Factors
chemical_list: D004676:Myelin Basic Protein; D012694:Serine; D010763:Phosphorylase b; D011494:Protein Kinases; D010764:Phosphorylase Kinase