乳酸脱氢酶的稳定性

Joachim Müller, Cornelia Klein
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引用次数: 5

摘要

用冻融法获得了猪心脏和肌肉以及鸡心脏和猪心脏乳酸脱氢酶的杂交体[1,2]。离子交换色谱对杂交产物的混合物进行了不同寻常的洗脱模式,即2 + 2杂交产物(H2PM2P和H2CH2P)在两个不同的峰中被洗脱。这些亚形态是由三种几何异构体的部分分解产生的。鸡心和猪心乳酸脱氢酶的杂交表现出三个不同水平的稳定性。H4P、HCH3P和H2CH2PI的特征变性温度为61.5℃;H2CH2PII和H3CHP为71°C, H4C为76.5°C。因此,对热变性的抵抗似乎是由四聚体酶中最不稳定的二聚体控制的。二聚体的稳定性排列与Arg241(鸡)和Asp57(鸡和猪)[3]在q接触区域内的附加离子对数目非常一致。乳酸脱氢酶热变性的速率决定步骤包括四聚体的两个q -触点中的一个的扭曲或解离。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Stability of lactate dehydrogenase

Hybrids of lactate dehydrogenases from pig heart and muscle and from chicken heart and pig heart were obtained by the freeze-thaw method [1,2]. Ion-exchange chromatography of the resulting mixtures of hybrids yielded unusual elution patterns, i.e., the 2 + 2 hybrids (H2PM2P and H2CH2P) were eluted in two separate peaks. These subforms were concluded to result from partial resolution of the three geometric isomers. The hybrids of chicken heart and pig heart lactate dehydrogenase showed three distinct levels of stability. The characteristic temperatures of denaturation were 61.5°C for H4P, HCH3P and H2CH2PI; 71°C for H2CH2PII and H3CHP and 76.5°C for H4C. The resistance towards thermal denaturation thus seemed to be governed by the least stable dimer within the tetrameric enzyme. The arrangement of stabilities of the dimers was in excellent agreement with the number of additional ion pairs between Arg241 (chicken) and Asp57 (chicken and pig) [3] within the Q-contact areas. The rate-determining step of thermal denaturation of lactate dehydrogenase was concluded to comprise the distortion or dissociation of one of two Q-contacts of the tetramer.

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