蛋白质-蛋白质相互作用：使用气动超速离心机通过沉降平衡分析伴刀豆球蛋白A与血清糖蛋白的相互作用。
Protein-protein interactions: analysis of the interaction of concanavalin A with serum glycoproteins by sedimentation equilibrium using an air-driven ultracentrifuge.
作者信息
Howlett G J, Roche P J, Schreiber G
出版信息
Arch Biochem Biophys. 1983 Jul 1;224(1):178-85. doi: 10.1016/0003-9861(83)90202-3.
An air-driven ultracentrifuge has been used for the quantitative analysis of the interaction of concanavalin A with a number of serum glycoproteins. Concanavalin A significantly affected the sedimentation equilibrium behavior of 125I-labeled human alpha 1-acid glycoprotein, rat alpha 1-acid glycoprotein, and rat transferrin containing two N-acetylneuraminic acid residues per molecule (Tf2). The weight-average molecular weight of the labeled component increased and there was a corresponding decrease in the concentration of the labeled component at the meniscus. In contrast, concanavalin A did not significantly alter the sedimentation equilibrium behavior of the 125I-labeled rat transferrin containing three N-acetyl neuraminic acid residues per molecule. Sedimentation equilibrium results for interacting mixtures of concanavalin A and labeled glycoprotein and at various concentrations of the competitive inhibitor alpha-methyl mannoside were analyzed in terms of a model. Values of 5 X 10(4), 2 X 10(5), and 6 X 10(5) M-1 were obtained for the equilibrium constants for the interaction of concanavalin A with Tf2, human alpha 1-acid glycoprotein, and rat alpha 1-acid glycoprotein, respectively.
一种气动超速离心机已被用于定量分析伴刀豆球蛋白A与多种血清糖蛋白之间的相互作用。伴刀豆球蛋白A显著影响了125I标记的人α1-酸性糖蛋白、大鼠α1-酸性糖蛋白以及每分子含有两个N-乙酰神经氨酸残基的大鼠转铁蛋白（Tf2）的沉降平衡行为。标记成分的重均分子量增加，且弯月面处标记成分的浓度相应降低。相比之下，伴刀豆球蛋白A并未显著改变每分子含有三个N-乙酰神经氨酸残基的125I标记的大鼠转铁蛋白的沉降平衡行为。根据一个模型分析了伴刀豆球蛋白A与标记糖蛋白的相互作用混合物在不同浓度竞争性抑制剂α-甲基甘露糖苷存在下的沉降平衡结果。伴刀豆球蛋白A与Tf2、人α1-酸性糖蛋白和大鼠α1-酸性糖蛋白相互作用的平衡常数分别为5×104、2×105和6×105 M-1。
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