Sculley M J, Treacy O B, Jeffrey P D
Department of Physical Biochemistry, John Curtin School of Medical Research, Australian National University, Canberra, ACT 2601, Australia.
Biophys Chem. 1984 Jan;19(1):39-47. doi: 10.1016/0301-4622(84)85004-8.
The use of bifunctional reagents to form cross-links between subunits in protein oligomers and subsequent disruption of noncovalent interactions with SDS allows comment upon the number of subunits and the symmetry in the original assembly. In existing treatments the number of equations needed to describe theoretically the proportions of all the cross-linked species that can be formed as a function of time in this way makes the analysis of the system unmanageable for proteins with more than four subunits. A method is presented that allows the required equations for any oligomer to be formulated as an algorithm suitable for solution by computer. Its application is illustrated with reference to experimental results obtained with two protein hexamers, Jasus hemocyanin and alpha-urease from jack bean.
使用双功能试剂在蛋白质寡聚体的亚基之间形成交联，随后用十二烷基硫酸钠（SDS）破坏非共价相互作用，可以对亚基数量和原始组装中的对称性进行评估。在现有处理方法中，要从理论上描述以这种方式随时间形成的所有交联物种的比例所需的方程数量，使得对于具有四个以上亚基的蛋白质，该系统的分析变得难以处理。本文提出了一种方法，可将任何寡聚体所需的方程制定为适合计算机求解的算法。文中通过参考从岩龙虾血蓝蛋白和刀豆α - 脲酶这两种蛋白质六聚体获得的实验结果来说明该方法的应用。
