Robertson P, Hiskey R G, Koehler K A
J Biol Chem. 1978 Sep 10;253(17):5880-3.
The determination of binding constants of metal ions to biomolecules is approachable via many techniques. Metal ion NMR spectroscopy is an alternative to more traditional techniques and is complementary to them, particularly in investigations of the interactions of metal ions with relatively small peptides containing multiple ionizing groups. The method requires relatively small amounts of material, is fairly fast, and is carried out at equilibrium. Our study has been of calcium and magnesium ion binding to gamma-carboxyglutamic acid (Gla)-containing peptides. Dissociation constants of approximately 0.6 mM for the binding of either metal ion to Z-D-Gla-D-Gla-OMe have been obtained. The procedure for determination of these constants via metal ion NMR is discussed.
通过多种技术可以测定金属离子与生物分子的结合常数。金属离子核磁共振光谱法是一种替代更传统技术的方法，并且与它们互补，特别是在研究金属离子与含有多个电离基团的相对较小的肽的相互作用时。该方法所需材料量相对较少，速度相当快，并且是在平衡状态下进行的。我们的研究是关于钙和镁离子与含γ-羧基谷氨酸（Gla）的肽的结合。已经获得了两种金属离子与Z-D-Gla-D-Gla-OMe结合的解离常数约为0.6 mM。讨论了通过金属离子核磁共振测定这些常数的程序。
