The lactate dehydrogenase of the icefish heart: biochemical adaptations to hypoxia tolerance.
Cardiac lactate dehydrogenase from the hemoglobin- and myoglobin-free antarctic icefish has been purified by affinity chromatography. Structural and kinetic properties of the enzyme were found close or identical to those of its skeletal muscle counterpart and other M-type lactate dehydrogenases. A model involving a dual oxidative-anaerobic metabolism of the icefish heart is proposed.
Feller
G
G
Laboratory of Biochemistry, University of Liege, Belgium.
Pauly
J P
JP
Smal
A
A
O'Carra
P
P
Gerday
C
C
D000064:Acclimatization; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000864:Antarctic Regions; D002846:Chromatography, Affinity; D003081:Cold Climate; D005399:Fishes; D000860:Hypoxia / Q000201:enzymology*; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000302:isolation & purification / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D009206:Myocardium / Q000201:enzymology*; D014337:Trout; D014508:Urea / Q000494:pharmacology
D000596:Amino Acids; D007527:Isoenzymes; D014508:Urea; D007770:L-Lactate Dehydrogenase