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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
Published on: January 16, 2012
Yak lactate dehydgogenase A4: purification, properties, and cDNA cloning
Yucai Zheng1, Xiaohui Si, Qinghua He
1College of Life Science and Technology, Southwest University for Nationalities, Chengdu, PR China. yucaizheng01@gmail.com
Bioscience, Biotechnology, and Biochemistry
|September 9, 2008
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.
