Chromatography proteins

Protein acidulant Protein additives Protein ammo acids a-l-Proteinase inhibitor Protein-based mimetics Protein Ca [42617-41-4] Protein channels Protein chromatography Protein crystal growth... 

Reversed-phase chromatography is widely used as an analytical tool for protein chromatography, but it is not as commonly found on a process scale for protein purification because the solvents which make up the mobile phase, ie, acetonitrile, isopropanol, methanol, and ethanol, reversibly or irreversibly denature proteins. Hydrophobic interaction chromatography appears to be the least common process chromatography tool, possibly owing to the relatively high costs of the salts used to make up the mobile phases. 

Gallant, S.R. and Cramer, S.M., Productivity and operating regimes in protein chromatography using low-molecular-mass displacers, J. Chromatogr. A, 771, 9, 1997. 

Chang, N. and Klibanov, A. M., Protein chromatography in neat organic solvents, Biotech. Bioeng., 39, 575, 1992. 

Now that you understand the basis for the interactions between functional groups in water, you also understand the basis for most interactions DNA-DNA, DNA-RNA, DNA-protein, RNA-protein, protein-protein, protein-ligand, enzyme-substrate (Get the picture ), antibody-antigen, protein-chromatography column—it s all the same stuff. 

Peak broadening in protein chromatography Theoretical aspects Anion Exchange disks [83]... 

Kenny, A. and Fowell, S. (eds) (1992) Practical protein chromatography, Humana Press, USA. 

Harris, D. A. (1992) Size-exclnsion high-performance liquid chromatography of proteins, in Methods in Molecular Biology, vol. 11 Practical Protein Chromatography (Kenney, A. and Powell, S., eds.), Humana, Clifton, NJ, pp. 223-236. 

Practical Protein Chromatography, Humana Press, Totowa, New Jersey... 

At about the same time, the field of protein separation and purification was undergoing rapid development. The introduction of materials for protein chromatography, such as cross-linked dextran, agarose, and polyacrylamide, provided a means to study protein-surface interactions, as well as to dramatically advance knowledge in protein biochemistry. 

The most useful information on the interactions of proteins with surfaces will come from studies analogous to those of protein chromatography, where well-characterized and understood proteins are studied with well-characterized surfaces of known functional group type and density. The information obtained is then analyz-able in such a way as to deduce interaction site densities and interaction energies. Only with such data in hand will we be able to begin to quantitatively treat and understand protein adsorption. 

With the development of neutral hydrophilic methacrylates in Prague, originally for contact lens applications in the early 60 s113>, considerable interest was generated in the application of these materials in the cardiovasular environment. The qualitative argument was that such soft, water-rich surfaces must be relatively non-traumatic to proteins and cells. The development of neutral hydrophilic polysaccharide-based particles for protein chromatography in the late 60 s provided evidence that such surfaces do indeed show minimal binding of proteins. 

Most literature on enzyme kinetics is devoted to initial rate data and the analysis of reversible effects on enzyme activity. In many applications and process settings, however, the rate at which the enzyme activity declines is of critical importance. This is especially true when considering its long-term use in continuous reactors. In such situations the economic feasibility of the process may hinge on the useful lifetime of the enzyme biocatalyst. The focus of this section is on the mechanisms and kinetics of loss of enzyme activity. It should also be recognised that the alteration of protein structure is central to the practical manipulation of proteins (e.g. precipitation, affinity and other forms of protein chromatography, and purification in general). 

M Leonard. New packing materials for protein chromatography. J Chromatogr B 699 3-27, 1997. 

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