title: Localization of the alpha-oxoacid dehydrogenase multienzyme complexes within the mitochondrion.
abstract: Bovine kidney mitochondria were separated into matrix and membrane fractions by treatment with digitonin and Lubrol PX. While malate dehydrogenase was found essentially in the matrix fraction, both the pyruvate and the alpha-oxoglutarate dehydrogenase multienzyme complexes remained bound to the inner membrane fraction and became solubilized only after repeated treatments with detergents. Thus both multienzyme complexes must be associated with the inner membrane rather than located within the matrix space.
authors: Physiologisch-chemisches Institut der Universität Tübingen, Germany.
authors: E
authors: E
authors: Maas
authors: H
authors: H
authors: Bisswanger
mesh_terms: D000818:Animals; D002417:Cattle; D003902:Detergents; D066298:In Vitro Techniques; D007655:Ketoglutarate Dehydrogenase Complex / Q000378:metabolism*; D007668:Kidney / Q000201:enzymology / Q000648:ultrastructure; D008291:Malate Dehydrogenase / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology* / Q000648:ultrastructure; D009097:Multienzyme Complexes / Q000378:metabolism*; D011768:Pyruvate Dehydrogenase Complex / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology
chemical_list: D003902:Detergents; D009097:Multienzyme Complexes; D011768:Pyruvate Dehydrogenase Complex; D008291:Malate Dehydrogenase; D007655:Ketoglutarate Dehydrogenase Complex