Purification and properties of pyruvate dehydrogenase kinase from bovine kidney.
Pyruvate dehydrogenase kinase was purified about 2,700-fold to apparent homogeneity from extracts of bovine kidney mitochondria. The kinase consists of two subunits (alpha beta) with molecular weights of 48,000 (alpha) and 45,000 (beta) as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Kinase activity resides in the alpha subunit. The alpha subunit is sensitive to proteolysis by chymotrypsin, whereas the beta subunit is selectively modified by trypsin. These observations, together with the results of peptide mapping, indicate that the two subunits are distinctly different proteins. It is proposed that the beta subunit is a regulatory subunit.
D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism; D007668:Kidney / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010663:Phenylmercury Compounds; D011494:Protein Kinases / Q000302:isolation & purification*; D017346:Protein Serine-Threonine Kinases; D000081382:Pyruvate Dehydrogenase Acetyl-Transferring Kinase; D012697:Serine Endopeptidases; D014357:Trypsin / Q000378:metabolism
D046911:Macromolecular Substances; D010446:Peptide Fragments; D010663:Phenylmercury Compounds; D000081382:Pyruvate Dehydrogenase Acetyl-Transferring Kinase; C002910:4-hydroxymercuribenzenesulfonate; D011494:Protein Kinases; D017346:Protein Serine-Threonine Kinases; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D014357:Trypsin