title: Autophosphorylation of lactate dehydrogenase.
abstract: Incubation of rabbit muscle lactate dehydrogenase in the presence of Mg[alpha-32p]ATP results in the incorporation of the label into the protein. The autophosphorylation reaction is strongly pH-dependent. The maximal phosphorylation is observed at pH 6.8 with 3-4 moles of phosphate bound per mole of tetrameric enzyme. The enzyme-phosphate complex is readily hydrolyzed by hydroxylamine.
authors.affiliation: A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
authors.forename: M V
authors.initials: MV
authors.lastname: Yasykova
authors.forename: L I
authors.initials: LI
authors.lastname: Ashmarina
authors.forename: V I
authors.initials: VI
authors.lastname: Muronetz
authors.forename: N K
authors.initials: NK
authors.lastname: Nagradova
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002850:Chromatography, Gel; D006863:Hydrogen-Ion Concentration; D019811:Hydroxylamine; D006898:Hydroxylamines / Q000494:pharmacology; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008274:Magnesium / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology; D010766:Phosphorylation; D011817:Rabbits
chemical_list: D006898:Hydroxylamines; D019811:Hydroxylamine; D000255:Adenosine Triphosphate; D007770:L-Lactate Dehydrogenase; D008274:Magnesium