Purification and Characterization of Pyruvate‐Dehydrogenase Phosphatase from Pig‐Heart Muscle

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Abstract
Pyruvate‐dehydrogenase phosphatase was extensively purified from pig heart muscle. The molecular weight was determined to be in the range between 92000 and 95000. By dodecylsulfate‐gel electrophoresis there was no indication for a subunit structure of the protein. The phosphatase is dependent on Mg2+ or Mn2+. Half‐maximal activity was obtained, in histidine buffer, at 2.5 mM MgCl2 and 1.8 mM MnCl2, respectively. Fluoride at a concentration of 0.6 mM inhibited phosphatase activity by 50% in the presence of Mg2+, but not of Mn2+. The enzyme was not affected by alkylating thiol‐reagents. Studies with sequestering agents suggest that pyruvate‐dehydrogenase phosphatase contains a metal which, besides Mg2+ or Mn2+, is essential for its function.

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