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Inactivation and conformational changes of lactate dehydrogenase M4 during unfolding in urea solutions

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2 Author(s)
Guo Yuyuan ; Department of biological science and biotechnology, tsinghua university, beijing 100084 ; Zhou Haimeng

The conforrrational changes, followed by fluorescerce emssion and exposure of buried SH groups, and the inactivation of lactate dehydrogenase M4 in urea so utions have been studied. The results show that inactivation occurs before noticeable conformational anal change can be detected. that can be suggested that the active sites of lactate dehydrogenase M4 also displ ay more conforrrational flexibility than the enzyme molecule as a whole.

Published in:

Tsinghua Science and Technology  (Volume:2 ,  Issue: 1 )