限制性内切酶ScaI与其底物的相互作用。
Interaction of the restriction endonuclease ScaI with its substrates.
作者信息
Kita K, Hiraoka N, Kimizuka F, Obayashi A, Kojima H, Takahashi H, Saito H
出版信息
Nucleic Acids Res. 1985 Oct 11;13(19):7015-24. doi: 10.1093/nar/13.19.7015.
Abstract
The kinetic constants of the site-specific endonuclease, ScaI, for various substrates were determined. We estimated Vmax and Km for octa-, deca-, dodeca-, and hexadecanucleotides and for plasmid pBR322 DNA. Vmax for these substrates were close, but Km were quite different (in decreasing order, octa- greater than deca-, dodeca-, hexadeca- greater than pBR322). The results were discussed with respect to the tertiary structure of substrate.
摘要
测定了位点特异性内切核酸酶ScaI对各种底物的动力学常数。我们估算了八聚体、十聚体、十二聚体和十六聚体寡核苷酸以及质粒pBR322 DNA的Vmax和Km。这些底物的Vmax相近，但Km差异很大（按降序排列，八聚体大于十聚体、十二聚体、十六聚体大于pBR322）。结合底物的三级结构对结果进行了讨论。
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