[Catalytic properties of cytoplasmic and mitochondrial aconitate hydratase from rat cardiomyocytes].
Enzymatic activity of aconitate hydratase (aconitase, EC 4.2.1.3) from the rat heart is localized in the cytoplasm (65%) and mitochondria (35%). Cytoplasmic and mitochondrial forms of aconitate hydratase were separated by ion-exchange chromatography on CM-Cellulose and CM-Sephadex. The two forms have similar molecular weight, optimal pH range, and spectral properties; however, they have different chromatography properties, Km for citrate and isocitrate, as well as sensitivity to Fe2+ ions.
Medvedeva
L V
LV
Voronezh State University, Universitetskaya pl. 1, Voronezh, 394693 Russia.
Popova
T N
TN
Artiukhov
V G
VG
Matasova
L V
LV
D000154:Aconitate Hydratase / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D002852:Chromatography, Ion Exchange / Q000379:methods; D019343:Citric Acid / Q000737:chemistry / Q000378:metabolism; D003593:Cytoplasm / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000378:metabolism; D007523:Isocitrates / Q000737:chemistry / Q000378:metabolism; D008297:Male; D008929:Mitochondria, Heart / Q000201:enzymology*; D008970:Molecular Weight; D032383:Myocytes, Cardiac / Q000201:enzymology*; D051381:Rats
D007523:Isocitrates; D019343:Citric Acid; C034219:isocitric acid; D007501:Iron; D000154:Aconitate Hydratase