The lactate dehydrogenase of the icefish heart: biochemical adaptations to hypoxia tolerance

Biochim Biophys Acta. 1991 Sep 20;1079(3):343-7. doi: 10.1016/0167-4838(91)90079-f.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acclimatization*
  • Amino Acids / analysis
  • Animals
  • Antarctic Regions
  • Chromatography, Affinity
  • Cold Climate
  • Fishes
  • Hypoxia / enzymology*
  • Isoenzymes
  • Kinetics
  • L-Lactate Dehydrogenase / isolation & purification
  • L-Lactate Dehydrogenase / metabolism*
  • Muscles / enzymology
  • Myocardium / enzymology*
  • Trout
  • Urea / pharmacology

Substances

  • Amino Acids
  • Isoenzymes
  • Urea
  • L-Lactate Dehydrogenase