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化学学报
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化学学报 ›› 2003, Vol. 61 ›› Issue (1): 95-99. 上一篇    下一篇

研究论文

微透析高效液相色谱法研究金属酶与小分子的相互作用

郭明;孔亮;厉欣;邹汉法   

  1. 中国科学院大连化学物理研究所国家色谱研究中心,大连(116011)
  • 发布日期:2003-01-15

Interaction of Metalloenzyme with Small Molecules Studied by Microdialysis/HPLC

Guo Ming;Kong Liang;Li Xin;Zou Hanfa   

  1. National Chromatography R. & A. Center, Dalian Insitue of Chemical Physics, Chinese Academy of Sciences,Dalian(116011)
  • Published:2003-01-15

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被引次数

19 | 1

将微透析（microdialysis)高效液相色谱法（high performance liquid chromatography,HPLC)联用技术应用于定量研究超氧化物歧化酶（superoxide dismutase)与组氨酸和组氨酸－金属离子配合物的相互作用。实验结果表明： Cu2Zn2SOD酶不仅与组氨酸，而且还可以与组氨酸－Co(Ⅱ）和组氨酸－Ni(Ⅱ)相互 作用，Cu2Zn2SOD酶中的部分Cu(Ⅱ)和Zn(Ⅱ)被诱导和置换出来，并相应地影响了 酶的活性；组氨酸－金属离子配合物的作用比组氨酸强，酶活性降低也更明显；酶 中结合的外来金属离子的量比从酶上被诱导和顶替下来的金属离子的量要少，说明 在溶液中有脱辅基酶的存在。

关键词: 金属, 酶, 分子, 固态配合物, 超氧化物歧化酶, 相互作用, 高速液相色谱

In this paper, a method of microdialysis coupled with high performance liquid chromatography (HPLC) was established to study the quantitative interaction of superoxide dismutase (Cu_2Zn_2SOD) with histidine and histidine-metal ion complexes. It was observed that not only histidine, but also histidine-Co(II) and histidine-Ni(II) could induce and substitute some Cu(II) and Zn(II) from Cu_2Zn_2SOD, eventually influence the activity of this metalloenzyme. Histidine- metal ion complexes have stronger ability than histidine to displace the bound metal ion from SOD. In addition, the amount of foreign metal ion binding to the SOD was less than that of metal ion lost from SOD. It obviously means that there was apoenzyme in the solution.

Key words: METAL, ENZYME, MOLECULAR, SOLID COMPLEX, SUPEROXIDE DISMUTASE, INTERACTIONS, HIGH-SPEED LIQUID CHROMATOGRAPHY

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