引用本文:
赖兵, 李颖, 曹傲能, 来鲁华. 古细菌RNase HII与金属离子结合的热力学研究[J]. 物理化学学报,
2001, 17(10): 865-867.
doi:
10.3866/PKU.WHXB20011001
Citation: Lai Bing, Li Ying, Cao Ao-Neng, Lai Lu-Hua. Thermodynamic Study on Binding of Archaebacterial RNase HII and Metal Ions[J]. Acta Physico-Chimica Sinica, 2001, 17(10): 865-867. doi: 10.3866/PKU.WHXB20011001
Citation: Lai Bing, Li Ying, Cao Ao-Neng, Lai Lu-Hua. Thermodynamic Study on Binding of Archaebacterial RNase HII and Metal Ions[J]. Acta Physico-Chimica Sinica, 2001, 17(10): 865-867. doi: 10.3866/PKU.WHXB20011001
古细菌RNase HII与金属离子结合的热力学研究
摘要:
RNase H是一种专一性水解RNA:DNA杂合链中RNA链的核糖核酸酶,它广泛存在于从原核生物到人的生物体中.本文通过等温滴定量热技术研究了Mg2＋,Mn2＋和Ca2＋与一种古细菌Methanococcus jannaschii中的II型RNase H结合的热力学.首次用这种方法获得了这一结合过程的热力学参数.并证实了这些金属离子与RNase HII按1∶1结合.为RNase HII酶反应机理和折叠研究提供了重要信息.
English
Thermodynamic Study on Binding of Archaebacterial RNase HII and Metal Ions
Abstract:
RNase H,a ribonuclease specifically degrades the RNA chain in RNA:DNA hybrid,exists vastly in organisms from procaryotic to humanic.We use isothermal titration calorimetry to study the binding thermodynamics of Mg2＋,Mn2＋,Ca2＋ to a type II RNase H from an archaeon:Methanococcus jannaschii.For the first time we obtain the thermodynamic parameters of this binding reaction and verify that these metal ions bind with RNase HII with a ratio of 1:1.This will give an important information for studying RNase HII reaction mechanism and folding properties.
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