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- W22278423 abstract "This chapter elaborates the regulation of heart muscle pyruvate dehydrogenase by phosphorylation/dephosphorylation reactions. Details of the possible subunit structure of the pig heart pyruvate dehydrogenase complex are shown. It is found that of the three enzymes catalyzing the overall reaction, only the decarboxylase shows a heterogeneous subunit composition. It is a tetramer consisting of two α, and two B subunits. The acetyltransferase as it is isolated is a polymer consisting of about 24 identical subunits which contain 1 mole covalently bound lipoyl residue/mole subunit. The incorporation of phosphate into pig heart pyruvate dehydrogenase, only into the α subunit of pyruvate decarboxylase. It is found that if phosphorylation of pyruvate dehydrogenase is stopped either before inactivation of the enzyme is complete, or after prolonged incubation of the enzyme with ATP-Mg2-, and the subunits of the complex are separated by SDS/polyacrylamide disc gel electrophoresis [32P] radioactivity and α subunit staining are coincident at either extent of phosphorylation." @default.
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- W22278423 date "1978-01-01" @default.
- W22278423 modified "2023-09-27" @default.
- W22278423 title "REGULATION OF HEART MUSCLE PYRUVATE DEHYDROGENASE BY PHOSPHORYLATION/DEPHOSPHORYLATION REACTIONS" @default.
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- W22278423 doi "https://doi.org/10.1016/b978-0-08-022623-1.50012-5" @default.
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