Determination of the surface tension of proteins I. Surface tension of native serum proteins in aqueous media

C.J. Van Oss , D.R. Absolom , A.W. Neumann , W. Zingg
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引用次数: 72

Abstract

The desorption patterns of serum proteins in hydrophobic chromatography suggest that serum proteins that remain immersed in an aqueous medium and do not become involved in a protein-air interface are very hydrophilic. Contact angle measurements on fairly thick layers of hydrated serum proteins, formed on ultrafiltration membranes, yield surface tensions that correlate well with the degree of hydrophilicity derived from desorption data obtained by hydrophobic chromatography. For further confirmation the absorptivity of four human serum proteins was measured with respect to surfaces of different polymers of various surface tensions, from solution in aqueous solvents of different surface tensions. The surface tension of the solvent from which a dissolved protein adsorbs to precisely the same extent onto all solid substrates (regardless of their surface tensions) is equal to the surface tension of that protein. The surface tensions found by the contact angle (first value given) and by the protein adsorption methods (second value given) were, in erg/cm2; α2-macroglobulin, 71.0, 71.0; serum albumin, 70.5, 70.2; immunoglobulin M, 69.5, 69.4; immunoglobulin G, 67.4, 67.7.

蛋白质表面张力的测定。天然血清蛋白在水介质中的表面张力
疏水色谱中血清蛋白的解吸模式表明,浸泡在水介质中且不参与蛋白质-空气界面的血清蛋白是非常亲水的。在超滤膜上形成的相当厚的水合血清蛋白层的接触角测量结果显示,表面张力与疏水色谱解吸数据得出的亲水性程度密切相关。为了进一步证实,在不同表面张力的水溶液中,测量了四种人血清蛋白对不同表面张力的不同聚合物表面的吸收率。溶解的蛋白质在所有固体底物上以完全相同的程度吸附的溶剂的表面张力(不管它们的表面张力如何)等于该蛋白质的表面张力。接触角(给定的第一个值)和蛋白质吸附法(给定的第二个值)得到的表面张力为,单位为erg/cm2;α2-巨球蛋白,71.0,71.0;血清白蛋白,70.5,70.2;免疫球蛋白M, 69.5, 69.4;免疫球蛋白G, 67.4, 67.7。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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