引用本文:	刘陶陶,王希成.铜离子对海参精氨酸激酶活力与结构的影响[J].海洋科学,2011,35(1):17-21.

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铜离子对海参精氨酸激酶活力与结构的影响
刘陶陶¹, 王希成^1,2
1.清华大学生命科学院;2.清华大学生命科学院蛋白质科学教育部重点实验室

摘要:

精氨酸激酶(Arginine kinase, EC2.7.3.3)是无脊椎动物能量代谢所必需的重要的酶。海参精氨酸激酶是一种特殊的双亚基精氨酸激酶。本文研究了在二价铜离子作用下, 海参精氨酸激酶催化活性与结构的变化。结果表明, 一定浓度的铜离子, 可以抑制精氨酸激酶的活力, 并引起酶二级结构与三级结构的变化, 引起疏水面暴露, 并导致酶的聚集。铜离子对精氨酸激酶的抑制作用与镁离子等其他二价金属离子有明显不同。

关键词: 精氨酸激酶(Arginine kinase, EC2.7.3.3) Cu²⁺ 聚沉去折叠

DOI：

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基金项目:

Effects of Cu²⁺ on Arginine kinase: activity changes, conformational changes, and aggregation

Abstract:

Arginine kinase (AK) plays an important role in the cellular energy metabolism of invertebrate. AK from sea cucumber Stichopus japonicus is dimeric. The effects of Cu²⁺ on AK were studied by measuring activity changes, kinetic time course of inactivity, far-UV circular dichroism spectra, fluorescence spectra, and turbidity changes at 400nm. These results suggested that Cu²⁺ caused AK inactivation accompanied by conformational change, exposure of hydrophobic surface, and aggregation. The effects of Cu²⁺ on AK are distinctive compared with other metal divalent ions.

Key words: Arginine kinase Cu²⁺ aggregation unfolding