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Autophosphorylation of lactate dehydrogenase
M V Yasykova1, L I Ashmarina, V I Muronetz
1A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
Biochemistry International
|May 1, 1987
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.