Yak lactate dehydgogenase A4: purification, properties, and cDNA cloning

Biosci Biotechnol Biochem. 2008 Sep;72(9):2448-51. doi: 10.1271/bbb.80208. Epub 2008 Sep 7.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Cattle / genetics*
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • DNA, Complementary / isolation & purification
  • Isoenzymes / genetics*
  • Isoenzymes / metabolism*
  • Kinetics
  • L-Lactate Dehydrogenase / genetics*
  • L-Lactate Dehydrogenase / isolation & purification*
  • L-Lactate Dehydrogenase / metabolism
  • Lactic Acid / isolation & purification
  • Models, Molecular
  • Molecular Sequence Data
  • Muscle, Skeletal / enzymology
  • Pyruvic Acid / isolation & purification
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • Isoenzymes
  • Lactic Acid
  • Pyruvic Acid
  • L-Lactate Dehydrogenase