Liquid-vapor interfacial tension of blood plasma, serum and purified protein constituents thereof

被引:47
作者
Krishnan, A
Wilson, A
Sturgeon, J
Siedlecki, CA
Vogler, EA
机构
[1] Penn State Univ, Dept Bioengn, University Pk, PA 16802 USA
[2] Penn State Univ, Dept Mat Sci & Engn, University Pk, PA 16802 USA
[3] Penn State Univ, Coll Med, Inst Biomed Engn, Dept Surg, Hershey, PA 17033 USA
关键词
protein adsorption; liquid-vapour interfacial tension; plasma; serum; blood proteins;
D O I
10.1016/j.biomaterials.2004.09.016
中图分类号
R318 [生物医学工程];
学科分类号
0831 ;
摘要
A systematic study of water-air (liquid-vapor, LV) interfacial tension gamma(\v), of blood plasma and serum derived from four different mammalian species (human, bovine, ovine and equine) reveals nearly identical concentration-dependence (dgamma(\v)/d ln C-B; where CB is plasma/serum dilution expressed in v/v concentration units). Comparison of results to a previously-published survey of purified human-blood proteins further reveals that dgamma(\v)/d ln C-B, of plasma and serum is surprisingly similar to that of purified protein constituents. It is thus concluded that any combination of blood-protein constituents will be substantially similar because dgamma(\v)/d In C-B of individual proteins are very similar. Experimental results are further interpreted in terms of a recently-developed theory emphasizing the controlling role of water in protein adsorption. Accordingly, the LV interphase saturates with protein adsorbed from bulk solution at a fixed weight-volume concentration (similar to436 mg/mL) independent of protein identity or mixture. As a direct consequence, dgamma(\v)/d ln C-B of purified proteins closely resembles that of mixed solutions and does not depend on the relative proportions of individual proteins comprising a mixture. Thus variations in the plasma proteome between species are not reflected in dgamma(\n)/d ln C-B nor is serum different from plasma in this regard, despite being depleted of coagulation proteins (e.g. fibrinogen). A comparison of pendant-drop and Wilhelmy-balance tensiometry as tools for assessing protein gamma(\v) shows that measurement conditions employed in the typical Wilhelmy plate approach fails to achieve the steady-state adsorption state that is accessible to pendant-drop tensiometry. (C) 2004 Elsevier Ltd. All rights reserved.
引用
收藏
页码:3445 / 3453
页数:9
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