Purification of malate dehydrogenase from chicken liver mitochondria. Existence of a small quantity of cytosolic isoenzyme.
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.
Gelpí
J L
JL
Departament de Bioquímica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
Domènech
C
C
Mazo
A
A
Cortés
A
A
Bozal
J
J
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*
D007527:Isoenzymes; D008291:Malate Dehydrogenase