Isoenzyme-specific thermostability of human cytosolic creatine kinase
Isoenzyme-specific thermostability of human cytosolic creatine kinase
复制标题
人胞质肌酸激酶的同工酶特异性热稳定性
DOI：
10.1016/j.ijbiomac.2010.03.025
复制
发表时间：
2010-07-01
影响因子：
8.2
通讯作者：
Zhou, Hai-Meng
中科院分区：
文献类型：
--
作者：
Gao, Yan-Song;Zhao, Tong-Jin;Zhou, Hai-Meng
肌酸激酶（CK）是参与细胞内能量稳态的关键酶。肌肉CK（MMCK）和脑CK（BBCK）的不同组织分布意味着它们在面临不同环境应力的条件下发挥作用。我们发现，MMCK和BBCK对热胁迫的稳定性和可逆性存在显著差异。MMCK比BBCK更稳定，BBCK仅略微稳定，并在略高于正常体温的温度下开始分解。MMCK的热失活是完全不可逆的，而BBCK在低于55 ℃的温度下是高度可逆的。这些稳定性的差异被认为与同工酶对不同组织环境的适应密切相关。(C)2010爱思唯尔有限公司版权所有。
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. (C) 2010 Elsevier B.V. All rights reserved.