Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stability.
Structure and activity of malate dehydrogenase from the extreme halophilic bacteria of the Dead Sea. 2. Inactivation, dissociation and unfolding at NaCl concentrations below 2 M. Salt, salt concentration and temperature dependence of enzyme stability.
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死海极端嗜盐细菌苹果酸脱氢酶的结构和活性。
DOI：
10.1111/j.1432-1033.1981.tb05543.x
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发表时间：
1981
期刊：
影响因子：
--
通讯作者：
H. Eisenberg
中科院分区：
文献类型：
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作者：
S. Pundak;H. Aloni;H. Eisenberg
嗜盐苹果酸脱氢酶的稳定性随着盐浓度的增加和温度的降低而增加。在高盐浓度下，各种盐的稳定性遵循霍夫迈斯特系列。酶失活速率与二聚酶解离成单体亚基和多肽链解折叠密切匹配，随后进行速度沉降、光散射和圆二色性测量。变性后，α-螺旋含量变为零。据信，天然酶的不寻常的水和盐结合特性（参见本杂志之前的论文）在酶解离和展开时大部分消失。因此，这些特性似乎与酶的完整结构有关。
The stability of halophilic malate dehydrogenase increases with increasing salt concentration and with decrease in temperature. Stabilization by various salts, at high salt concentrations, follows the Hofmeister series. The enzyme inactivation rates closely match dissociation of the dimeric enzymes into monomeric subunits and unfolding of the polypeptide chains, as followed by velocity sedimentation, light scattering and circular dichroism measurements. The alpha-helix content goes to zero upon denaturation. Unusual water and salt binding properties of the native enzyme (cf. preceding paper, in this journal) are believed to be largely lost upon enzyme dissociation and unfolding. The properties thus seem to be associated with the intact structure of the enzyme.
高分子材料对酶促反应的附加作用
DOI：
--
发表时间：
2004
期刊：
影响因子：
--
作者：
T. Takada;T. Shinozaki;Y. Kondo;T. Hirai,;T. Takada. T. Hirai,
通讯作者：
T. Takada. T. Hirai,