Yak lactate dehydgogenase A4: purification, properties, and cDNA cloning.
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.
Zheng
Yucai
Y
College of Life Science and Technology, Southwest University for Nationalities, Chengdu, PR China. yucaizheng01@gmail.com
Si
Xiaohui
X
He
Qinghua
Q
Jin
Suyu
S
Hong
Jian
J
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D002417:Cattle / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D007527:Isoenzymes / Q000235:genetics* / Q000378:metabolism*; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000235:genetics* / Q000302:isolation & purification* / Q000378:metabolism; D019344:Lactic Acid / Q000302:isolation & purification; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000201:enzymology; D019289:Pyruvic Acid / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D007527:Isoenzymes; D019344:Lactic Acid; D019289:Pyruvic Acid; D007770:L-Lactate Dehydrogenase