Professor J.Th.G. Overbeek on his eightieth birthday.
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Biomedical subjects
Publications and source records attributed to J Lyklema.
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In this paper we report a new set of thermodynamic linkage relations for the binding of electrolyte by proteins. The relations are derived for protein solutions in membrane equilibrium with a reference solution, allowing a phenomenological definition of ion binding. This is an extension of Wyman's linkage theory. The theory is applied to the electrolyte dependence of proton titration curves for bovine serum albumin in KCl solution (C. Tanford, S. A. Swanson and W. S. Shore, J. Am. Chem. Soc. 77 (1955) 6414). The curves are re-analysed in terms of Esin-Markov coefficients. In addition, we discuss the interpretation of the phenomenological K+ and Cl- binding numbers in terms of a two-state binding model, in which part of the ions are thought to adsorb on specific sites at the protein surface and/or part in the diffuse layer. It is shown that the electrolyte binds largely in the diffuse layer, especially when the protein surface charge is high.
An experimental analysis of charge regulation in protein adsorption is presented. The model system consists of colloidal particles of the slightly water soluble salt silver iodide as the adsorbent and the protein bovine serum albumin as the adsorbate. Protein adsorption experiments corroborate earlier findings that albumin adsorbs maximally close to the isoelectric point of the protein. The adsorption is reversible with respect to protein-protein exchange. The charge regulation is studied by novel potentiometric titrations. The Galvani potential of the adsorbent, partially covered with protein, is varied by the addition of AgNO3/KI while the pH is kept constant by means of a pH-stat. It is shown that the ion co-adsorption is a linear decreasing function of the blank surface charge density. The results are consistent with thermodynamics: for the first time a few phenomenological linkage relations between the ion co-adsorptions and chemical potentials are verified experimentally. The charge regulation is interpreted in terms of a contact layer model, which explains the ion co-adsorption by compounded ion exchange equilibria in the small layer of atomic contact between adsorbed protein and surface.
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A previously developed self-consistent field theory to describe the equilibrium properties of lipid-like membranes is extended to allow the presence of inhomogeneities parallel to the membrane. Conformations of lipid molecules and foreign ('guest') molecules in the membrane are obtained by step-weighted random walk generation of the chains on a lattice, where the theory is made two-dimensional to account for the parallel inhomogeneities. No pre-assigned positions of the head groups, or other parts of the molecules, are introduced. Nearest neighbor interactions are accounted for through Flory-Huggins type interaction parameters. The theory is applied to the incorporation of trans-membrane molecules and conditions for channel formation are discussed. Lateral phase separation in membranes consisting of non-mixing lipids is also considered. Water only slightly enriches the boundary between the two lipid regions. The aliphatic chains are very well able to smoothly cover inhomogeneities in the bilayer. No indications of instability of the membrane due to the induced inhomogeneities are found.
Bacterial adhesion in natural and artificial systems has been critically reviewed to investigate the influences exerted by the presence of interfaces. Numerous investigations have demonstrated that, in the presence of a solid phase, the activity of bacterial cultures is changed. Reviewing relevant literature, two problems were encountered. One is of an experimental nature. Due to lack of similarity in experimental conditions, disparate experiments often cannot be compared; their results may even appear conflicting. The other problem is of an interpretational nature: several hypothetical theories exist which try to explain the effect of surfaces on microbial activity. These theories often confuse changes in the medium and limitations in mass transfer which are due to the presence of solid surfaces (indirect influences) with changes in cell properties (direct influences). Whenever a surface is reported to influence the metabolism of bacteria, the action is found almost exclusively to be due to changes in the medium or environment and is therefore indirect. Based on data reported in the literature, and by using thermodynamic and kinetic considerations, it is concluded that so far neither experimental nor theoretical evidence exists for a direct influence of interfaces on microbial activity.
In this study, the adhesion of bacteria differing in surface hydrophobicity was investigated. Cell wall hydrophobicity was measured as the contact angle of water on a bacterial layer collected on a microfilter. The contact angles ranged from 15 to 70 degrees. This method was compared with procedures based upon adhesion to hexadecane and with the partition of cells in a polyethylene glycol-dextran two-phase system. The results obtained with these three methods agreed reasonably well. The adhesion of 16 bacterial strains was measured on sulfated polystyrene as the solid phase. These experiments showed that hydrophobic cells adhered to a greater extent than hydrophilic cells. The extent of adhesion correlated well with the measured contact angles (linear regression coefficient, 0.8).