Function of cytoplasmic NAD-dependent malate dehydrogenase from rat myocardium under conditions of ischemia.
NAD-dependent malate dehydrogenase activity decreased by 2.7 times in the myocardium of rats with experimental ischemia. Cytoplasmic NAD-dependent malate dehydrogenase from intact and ischemic rat heart was purified by 91.4 and 95.5 times. We compared kinetic characteristics and regulation of enzyme activity by Fe(2+), Cu(2+), Ca(2+), hydrogen peroxide, and glutathione under normal and pathological conditions.
Safonova
O A
OA
Voronezh State University. solga@bio.vsu.ru
Popova
T N
TN
Artyukhov
V G
VG
Matasova
L V
LV
D000818:Animals; D002118:Calcium / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D003300:Copper / Q000378:metabolism; D003593:Cytoplasm / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005978:Glutathione / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism; D007501:Iron / Q000378:metabolism; D007511:Ischemia / Q000378:metabolism*; D007700:Kinetics; D008291:Malate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D008297:Male; D009206:Myocardium / Q000201:enzymology*; D051381:Rats; D011922:Rats, Mutant Strains
D003300:Copper; D006861:Hydrogen Peroxide; D007501:Iron; D008291:Malate Dehydrogenase; D005978:Glutathione; D002118:Calcium