title: Purification of malate dehydrogenase from chicken liver mitochondria. Existence of a small quantity of cytosolic isoenzyme.
abstract: 1. A new purification method for chicken liver mitochondrial malate dehydrogenase is described. The application of affinity chromatography through 5'AMP-Sepharose and Blue-Sepharose permits to obtain homogeneous preparations, with good yields (47%), in a short time (48 hr). 2. The 5'AMP-Sepharose chromatography reveals the presence of two malate dehydrogenase species in the mitochondrial extracts. 3. A comparative study of these forms point out the cytosolic nature of the minority form and suggests that its presence could be due to a slight interaction of the cytosolic malate dehydrogenase with mitochondrial membranes.
authors.affiliation: Departament de Bioquímica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
authors.forename: J L
authors.initials: JL
authors.lastname: Gelpí
authors.forename: C
authors.initials: C
authors.lastname: Domènech
authors.forename: A
authors.initials: A
authors.lastname: Mazo
authors.forename: A
authors.initials: A
authors.lastname: Cortés
authors.forename: J
authors.initials: J
authors.lastname: Bozal
mesh_terms: D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D003600:Cytosol / Q000201:enzymology; D007527:Isoenzymes / Q000302:isolation & purification*; D008291:Malate Dehydrogenase / Q000302:isolation & purification*; D008930:Mitochondria, Liver / Q000201:enzymology*
chemical_list: D007527:Isoenzymes; D008291:Malate Dehydrogenase