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
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Acclimatization*
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Amino Acids / analysis
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Animals
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Antarctic Regions
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Chromatography, Affinity
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Cold Climate
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Fishes
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Hypoxia / enzymology*
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Isoenzymes
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Kinetics
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L-Lactate Dehydrogenase / isolation & purification
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L-Lactate Dehydrogenase / metabolism*
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Muscles / enzymology
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Myocardium / enzymology*
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Trout
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Urea / pharmacology
Substances
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Amino Acids
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Isoenzymes
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Urea
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L-Lactate Dehydrogenase