Yak Lactate Dehydgogenase A4: Purification, Properties, and cDNA Cloning

Yucai ZHENG; Xiaohui SI; Qinghua HE; Suyu JIN; Jian HONG

doi:10.1271/bbb.80208

This article has now been updated. Please use the final version.

Yak Lactate Dehydgogenase A4: Purification, Properties, and cDNA Cloning

Yucai ZHENG, Xiaohui SI, Qinghua HE, Suyu JIN, Jian HONG

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Keywords: yak, lactate dehydrogenase A, purification, molecular adaptation

JOURNAL FREE ACCESS Advance online publication

Article ID: 80208

DOI https://doi.org/10.1271/bbb.80208

The final version of this article is now available: Vol. 72 (2008) , No. 9 p.2448

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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.

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