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Isoenzyme-specific thermostability of human cytosolic creatine kinase.

Abstract：

:Creatine kinase (CK) is a key enzyme involved in intracellular energy homeostasis. The distinct tissue distribution of muscle CK (MMCK) and brain CK (BBCK) implies that they function under conditions facing dissimilar environmental stresses. We found that MMCK and BBCK were significantly different in their stability and reversibility against heat stress. MMCK was more stable than BBCK, and BBCK was only marginally stable and began to inactivate at temperatures just above normal body temperature. The thermal inactivation of MMCK was fully irreversible, whereas that of BBCK was highly reversible at temperatures below 55 degrees C. These differences in stability were proposed to be closely correlated to the isoenzymes' adaptation to the distinct tissue environments.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Gao YS,Zhao TJ,Chen Z,Li C,Wang Y,Yan YB,Zhou HM

doi

10.1016/j.ijbiomac.2010.03.025

subject

Has Abstract

pub_date

2010-07-01 00:00:00

pages

27-32

issue

1

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(10)00118-2

journal_volume

47

pub_type

杂志文章

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