高等学校化学学报

高等学校化学学报 ›› 2003, Vol. 24 ›› Issue (8): 1346.

• 论文 • 上一篇    下一篇

稀土离子对钙调蛋白与单克隆抗体分子识别的影响

李伟国1, 祁超1,2, 杜丽2, 刘立岩1, 赵大庆1   

  1. 1. 中国科学院长春应用化学研究所稀土化学与物理开放实验室, 长春 130022;
    2. 中国人民解放军军需大学生物化学教研室, 长春 130062
  • 收稿日期:2002-09-19 出版日期:2003-08-24 发布日期:2003-08-24
  • 通讯作者: 赵大庆(1963年出生),男,博士,研究员,博士生导师,主要从事生物无机化学研究.
  • 基金资助:

    国家自然科学基金重大项目(批准号:29890280)资助

Influence of Rare Earth Irons on the Molecular Recognition Between Calmodulin and Monoclonal Antibody

LI Wei-Guo1, QI Chao1,2, DU Li2, LIU Li-Yan1, ZHAO Da-Qing1   

  1. 1. Key Laboratory of Rare Earth Chemistry and Physics, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022, China;
    2. Department of Biochemistry, Quartermaster University of PLA, Changchun 130062, China
  • Received:2002-09-19 Online:2003-08-24 Published:2003-08-24

PDF (PC)

被引次数

15

摘要： 分别采用酶联免疫吸附(ELISA)法和荧光标记技术比较了Ca2+,La3+,Eu3+和Yb3+离子对钙调蛋白与单克隆抗体2C3之间分子识别的影响.结果表明,金属离子与钙调蛋白作用后会诱导其发生不同的构象变化,并进一步影响到钙调蛋白与单克隆抗体2C3分子之间的结合强度.当钙调蛋白分别与La3+,Eu3+,Yb3+作用后,它与单抗2C3分子之间的解离常数为(26.8±2.5),(21.8±3.4)和(64.8±5.1)nmol/L,而结合Ca2+前后的钙调蛋白与单抗分子的解离常数分别为(177.2±2.8)和(157±4.2)nmol/L.这一结果表明,稀土离子诱导钙调蛋白发生的构象变化明显不同于钙离子的作用,这种差异可能是稀土与钙离子对钙调蛋白调控作用表现出差别的原因.

关键词: 稀土离子, 钙调蛋白, 单克隆抗体, 分子识别

Abstract: The molecular recognitions between monoclonal antibody 2C3 and calmodulin saturated with different metaLIons(La3+, Eu3+, Yb3+and Ca2+) were investigated by the enzyme linked immunosorbent assay(ELISA) and labeled fluorescence spectroscopy.The results indicate that after binding with different metaLIons, the calmodulin undergoes different conformational changes, which have a significant effect on its recognition ability to a metaLIon induced conformation-specific monoclonal antibody.The dissociation constants between the antibody and the calmodulin saturated with La3+, Eu3+, Yb3+are (26.8±2.5), (21.8±3.4) and (64.8±5.1) nmol/L, respectively, while the dissociation constants between the antibody and Ca2+-CaMor apoCaMare (157±4.2) and (177.2±2.8) nmol/L, respectively.This result indicates lanthanide-induced conformational changes of calmodulin are not similar with that induced by calcium, which maybe account for the facts that lanthanide and calcium ions lead to different effects on the regulating function of calmodulin in biological systems.

Key words: Rare earth ion, Calmodulin protein, Monoclonal antibody, Molecular recognition

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