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Protein aqueous

Fig. 14. Circles typical NMRD data (water longitudinal relaxation rates in a protein aqueous solution adapted from ref. (55)).The curve corresponds to a lorentzian function with tq deduced from the half-height of the experimental data. Note... Fig. 14. Circles typical NMRD data (water longitudinal relaxation rates in a protein aqueous solution adapted from ref. (55)).The curve corresponds to a lorentzian function with tq deduced from the half-height of the experimental data. Note...
The formation of polymer-polymer complexes as a rule is observed in aqueous media5,33. The viscosity of complexes in water is about 0.05-0.10 dl/g and close to that of globular proteins. Aqueous solutions have some features low intrinsic viscosity values are independent of the matrix molecular weight, the absence both of the concentration dependence of the reduced viscosity and the polyelectrolyte anomaly, and high values (about 30 s) of the sedimentation constant. [Pg.109]

Flexible yellowish films with low moisture resistance properties formed from soy protein aqueous dispersions upon heating... [Pg.554]

Keywords Protein Aqueous mixed solvent Preferential binding parameter Solubility... [Pg.261]

Keywords Protein Aqueous polyethylene glycol Preferential binding parameter Solubility Fluctuation theory... [Pg.272]

For the extraction of proteins, aqueous two-phase systems (ATPS) are preferred over organic solvents, which usually denature the proteins and render them biologically inactive. They consist of polyethylene glycol (PEG), and a salt (e.g., potassium phosphate) or dextran in water. At concentrations above a critical value, the mixture separates into two phases—one rich in PEG and the other in dextran or salt. In industrial systems, salts are more commonly used because they are relatively inexpensive as compared to dextran. The MW, charge and surface properties of the protein decide how the protein partitions in the system. The nature of the phase components, the MW of the polymer, and the concentration and type of salt used also affect the distribution. ... [Pg.226]

Lipid oxidation effect on meat proteins Aqueous extracts of beef Centrifugation of aqueous extract... [Pg.382]

As an example, it is useful to recall protein solutions. Protein molecules can be quite large for example, a lysozyme molecule is an ellipsoid with dimensions 3x4x5 nm, similar to nanoparticles (they are in fact nanoparticles). Protein aqueous solutions have seen significant smdy in the recent past because it is desirable to form protein crystals from solution for strucmral analysis. Such a system contains not only the protein molecule and the water solvent but usually dissolved ions which dissociate and a variable pH. Moreover, the protein molecule may have a variety of surface states that affect its interaction with other protein molecules as well as the water. The lesson here is that often the system is too complex and an effective inter-particle interaction potential must be prescribed. Such a procedure often works because the number concentration of the large protein molecules or nanoparticles is far less than that of the other constituents. [Pg.49]

Ikkai. F. Naito, S. Dynamic light scattering and circular dichroism studies on heat-induced gelation of hard-keratin protein aqueous solutions. Biomacromolecules 2002. 3,... [Pg.803]

Concentrations, expressed per heme, were determined by the Drabkin method and were all close to 18 mM. Concentrations of.CO--heme were also determined breaking the cells in distilled water and using known extinction coefficient of CO-hemoglobin results of both methods were invariably found to be equal in the experimental error. Magnetic volume susceptibility measurements were performed with our superconducting susceptometer (25) as described elsewhere (23). The overall accuracy of the method for protein aqueous solutions referred to calibrations with pure deoxygenated water is 7x10" cgs units, or 1/1000 of the volume susceptibility of water. [Pg.252]

Protein Contact angle of fluorocarbon drop on protein layer in 0.15m HCl Interfaclal free energy at protein-aqueous interface (MN/rn )... [Pg.237]


See other pages where Protein aqueous is mentioned: [Pg.102]    [Pg.228]    [Pg.227]    [Pg.228]    [Pg.462]    [Pg.187]    [Pg.255]    [Pg.218]    [Pg.363]    [Pg.15]    [Pg.310]    [Pg.1477]    [Pg.175]    [Pg.238]    [Pg.54]    [Pg.236]   
See also in sourсe #XX -- [ Pg.51 ]




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