伴刀豆球蛋白A的pH依赖性构象变化
pH-dependent conformational changes of concanavalin A.
作者信息
Zand R, Agrawal B B, Goldstein I J
出版信息
Proc Natl Acad Sci U S A. 1971 Sep;68(9):2173-6. doi: 10.1073/pnas.68.9.2173.
Abstract
The pH dependence of the conformation of concanavalin A has been studied by means of optical rotatory dispersion and circular dichroism spectroscopy. At pH 2.9, 5.0, and 7.0, the major contribution to organized structure appears to be the beta conformation. At pH 9.1, the conformation of concanavalin A approaches the random coil or unordered form. No evidence could be found for the presence of any significant amount of alpha helix. The pH of maximum precipitin-like activity of concanavalin A is paralleled by the pH dependence of the parameter b(0) in the Moffitt equation.
摘要
已通过旋光色散和圆二色光谱法研究了伴刀豆球蛋白A构象的pH依赖性。在pH 2.9、5.0和7.0时，对组织结构的主要贡献似乎是β构象。在pH 9.1时，伴刀豆球蛋白A的构象接近无规卷曲或无序形式。未发现存在任何大量α螺旋的证据。伴刀豆球蛋白A的最大沉淀素样活性的pH值与莫菲特方程中参数b(0)的pH依赖性平行。
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