Adsorption Behavior of Cytochrome c, Myoglobin and Hemoglobin in a Quartz Surface Probed Using Slab Optical Waveguide (SOWG) Spectroscopy.

DOI PDF Web Site Web Site Web Site ほか1件をすべて表示 一部だけ表示 被引用文献15件 参考文献73件

この論文をさがす

抄録

Slab optical waveguide (SOWG) spectroscopy was used to observe the adsorption behavior of three important heme proteins, namely cytochrome c, myoglobin and hemoglobin, in a quartz surface. Using prism-coupled polychromatic visible light propagated into a quartz waveguide by internal total reflection, the real-time monitoring of evanescent wave absorption revealed a strong dependence of the protein-surface interaction on the protein concentration, the solution pH and the ionic strength. For the three proteins studied, the absorbance-bulk concentration ratio was higher at low bulk concentrations, and decreased at higher concentrations. For cytochrome c and myoglobin, the absorbance approached a limiting value, but buffered hemoglobin surprisingly did not show any indication of forming a signal plateau. Moreover, the slow introduction of protein into the solution lessened the total adsorbed amount per unit area. These observations suggested a possible conformational transition of the protein molecules at the quartz surface after adsorption. For a bulkier protein, hemoglobin, adsorption onto the quartz surface was enhanced in the presence of a phosphate buffer, while the opposite effect was observed for the smaller cytochrome c and myoglobin molecules. The results of pH studies concurred with the electrostatic interactions predicted from the isoelectric data of proteins and the quartz surface.

収録刊行物

  • Analytical Sciences

    Analytical Sciences 19 (2), 199-204, 2003

    社団法人 日本分析化学会

被引用文献 (15)*注記

もっと見る

参考文献 (73)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ