Abstract
Lactate dehydrogenase A4 (LDH-A4) was purified for yak skeletal muscle. Michaelis constant (Km) analysis showed that yak LDH-A4 for pyruvate was significantly higher than that of cattle. cDNA cloning of LDH-A revealed two amino acid substitutions between yak and cattle. We suggest that the higher Km of yak LDH-A4 might be a result of molecular adaptation to a hypoxic environment.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Animals
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Cattle / genetics*
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Cloning, Molecular
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DNA, Complementary / genetics
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DNA, Complementary / isolation & purification
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Isoenzymes / genetics*
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Isoenzymes / metabolism*
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Kinetics
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L-Lactate Dehydrogenase / genetics*
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L-Lactate Dehydrogenase / isolation & purification*
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L-Lactate Dehydrogenase / metabolism
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Lactic Acid / isolation & purification
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Models, Molecular
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Molecular Sequence Data
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Muscle, Skeletal / enzymology
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Pyruvic Acid / isolation & purification
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Sequence Homology, Amino Acid
Substances
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DNA, Complementary
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Isoenzymes
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Lactic Acid
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Pyruvic Acid
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L-Lactate Dehydrogenase