[Purification of the pyruvate dehydrogenase complex from bovine adrenal cortex mitochondria]

Isolation of the pyruvate dehydrogenase complex from bovine adrenal cortex and its purification including fractionation by polyethyleneglycol, ultracentrifugation and gel filtration on Sepharose 4B is described. The preparation obtained having the specific activity of 4,5 U/mg was purified 370-fold with a yield of 37%. Under polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate the pyruvate dehydrogenase complex is degraded into 4 protein fractions with the mobility corresponding to the molecular weights of 74 000, 56 000, 42 000 and 37 000.