Armstrong J M, McKenzie H A
Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC, Australia.
J Protein Chem. 2001 Apr;20(3):255-63. doi: 10.1023/a:1010960227494.
The use of the analytical ultracentrifuge to study nonideal behavior of macromolecules in multicomponent systems is discussed, noting the value of interference optics to extend the range of concentrations of macromolecule that may be studied. The choice of appropriate theory in the treatment of experimental data is examined, using a study of bovine serum albumin (BSA) in 7 M urea at pH 3.3 as an example. Under these conditions BSA undergoes extensive unfolding and exhibits marked nonideality, with the binding of approximately 200 molecules of urea per molecule of BSA.
讨论了使用分析超速离心机研究多组分体系中大分子的非理想行为，并指出干涉光学在扩展可研究大分子浓度范围方面的价值。以pH 3.3的7 M尿素中牛血清白蛋白（BSA）的研究为例，考察了处理实验数据时适当理论的选择。在这些条件下，BSA发生广泛的去折叠并表现出明显的非理想性，每分子BSA结合约200个尿素分子。
