AGRIS - International System for Agricultural Science and Technology

Advanced Search

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

2008

ZHENG, Yucai | SI, Xiaohui | He, Qinghua | JIN, Suyu | Hong, Jian

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.

AGROVOC Keywords

amino acids biotechnology cattle lactate dehydrogenase lactic acid purification pyruvic acid yak yaks

Bibliographic information

Published in

Bioscience, biotechnology, and biochemistry

Volume 72 Issue 9 Pagination 2448 - 2451 ISSN 1347-6947

Publisher

Japan Society for Bioscience, Biotechnology, and Agrochemistry

Other Subjects

Lactate dehydrogenase a; Skeletal muscle; Enzyme kinetics; Molecular adaptation

Language

English

Note

Nal-ap-2-clean

Type

Journal Article; Text

In AGRIS since: 2024-02-28

Format: MODS

Data Provider

This bibliographic record has been provided by National Agricultural Library

Discover this data provider's collection in AGRIS

Links

DOI DOI http://dx.doi.org/10.1271/bbb.80208

Lookup at Google Scholar

If you notice any incorrect information relating to this record, please contact us at [email protected]