The monomer-dimer equilibrium of the protein /?-la&globulin under neutral conditions appears to influence the rejection and the osmotic pressure build-up, both phenomena closely related to ultrafiltration. Rejection measurements indicate different rejections for the/3-lactoglobulin mono-mers and dimers: the membrane rejects the dimer almost completely and the monomer only par-tially. The osmotic pressure turns out to be highly dependent on the protein concentration. A good agreement, up to high concentrations, is found between experimental data and theoretical osmotic pressures, calculated by taking into account the state of association, the excluded volume and the Donnan effects. The effect of changes in pH on the osmotic pressure has ...
The flux decline behaviour of some charged proteins and of binary mixtures of charged solutes during...
The flux decline behaviour of some charged proteins and of binary mixtures of charged solutes during...
It was studied how protein-protein and protein-membrane interactions influence the filtration perfor...
The monomer-dimer equilibrium of the protein β-lactoglobulin under neutral conditions appears to inf...
Extending the understanding of the Physical Phenomenon of Crowded and Concentrated Protein Osmotic P...
Protein-protein interactions are essential for the understanding of biological processes. Specific p...
Solutions containing dextran and solutions containing mixtures of dextran +ß-lactoglobulin are studi...
Examination of the protein crystallization process involves investigation of the liquid and solid st...
In this study the effects of ionic strength and PH on ultrafiltration of protein solutions are exami...
The free-solvent model has been shown to have excellent predictability of the osmotic pressure for s...
The membrane concentration osmometer coupled with multiple sample preparations has been used for ove...
Applying small-angle X-ray scattering in combination with liquid-state theory, we determined the int...
The occurrence at 0.1-0.01 m ionic strength of an aspecific ion-exclusion effect at the membrane dur...
The free-solvent-based (FSB) model and osmotic pressure were used to probe the ion binding and prote...
The interaction of proteins (ß-lactoglobulin, Bovine Serum Albumin (BSA), gelatins and whey protein ...
The flux decline behaviour of some charged proteins and of binary mixtures of charged solutes during...
The flux decline behaviour of some charged proteins and of binary mixtures of charged solutes during...
It was studied how protein-protein and protein-membrane interactions influence the filtration perfor...
The monomer-dimer equilibrium of the protein β-lactoglobulin under neutral conditions appears to inf...
Extending the understanding of the Physical Phenomenon of Crowded and Concentrated Protein Osmotic P...
Protein-protein interactions are essential for the understanding of biological processes. Specific p...
Solutions containing dextran and solutions containing mixtures of dextran +ß-lactoglobulin are studi...
Examination of the protein crystallization process involves investigation of the liquid and solid st...
In this study the effects of ionic strength and PH on ultrafiltration of protein solutions are exami...
The free-solvent model has been shown to have excellent predictability of the osmotic pressure for s...
The membrane concentration osmometer coupled with multiple sample preparations has been used for ove...
Applying small-angle X-ray scattering in combination with liquid-state theory, we determined the int...
The occurrence at 0.1-0.01 m ionic strength of an aspecific ion-exclusion effect at the membrane dur...
The free-solvent-based (FSB) model and osmotic pressure were used to probe the ion binding and prote...
The interaction of proteins (ß-lactoglobulin, Bovine Serum Albumin (BSA), gelatins and whey protein ...
The flux decline behaviour of some charged proteins and of binary mixtures of charged solutes during...
The flux decline behaviour of some charged proteins and of binary mixtures of charged solutes during...
It was studied how protein-protein and protein-membrane interactions influence the filtration perfor...