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Purification protein

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. [Pg.47]

Table 2. Ion-Exchange Groups Used in Protein Purification ... Table 2. Ion-Exchange Groups Used in Protein Purification ...
Another example is the purification of a P-lactam antibiotic, where process-scale reversed-phase separations began to be used around 1983 when suitable, high pressure process-scale equipment became available. A reversed-phase microparticulate (55—105 p.m particle size) C g siUca column, with a mobile phase of aqueous methanol having 0.1 Af ammonium phosphate at pH 5.3, was able to fractionate out impurities not readily removed by hquid—hquid extraction (37). Optimization of the separation resulted in recovery of product at 93% purity and 95% yield. This type of separation differs markedly from protein purification in feed concentration ( i 50 200 g/L for cefonicid vs 1 to 10 g/L for protein), molecular weight of impurities (<5000 compared to 10,000—100,000 for proteins), and throughputs ( i l-2 mg/(g stationary phasemin) compared to 0.01—0.1 mg/(gmin) for proteins). [Pg.55]

S. M. Wheelwright, Protein Purification Design and Scale-up of Downstream Processing, Hanser PubHshers, Munich, Germany, 1991, pp. 1—9, 61, 213—217. [Pg.57]

L. Hagel, "Gel Filtration" in J-C. Janson and L. Ryden, ed.. Protein Purification Principles, High Resolution Methods, and Applications, VCH Pubhshers,... [Pg.58]

Other Applications. Polyacrylamides are used in many additional appUcations including soil modification (138), dust control (139,140), humidity control (141), protein purification (142), removal of barium from wastewater (143), and removal of arsenic from hydrocarbons (144). Polyacrylamides have been used for many years in sugar manufacture and textile treatment. [Pg.144]

The methods involved in the production of proteins in microbes are those of gene expression. Several plasmids for expression of proteins having affinity tails at the C- or N-terminus of the protein have been developed. These tails are usefiil in the isolation of recombinant proteins. Most of these vectors are commercially available along with the reagents that are necessary for protein purification. A majority of recombinant proteins that have been attempted have been produced in E. Coli (1). In most cases these recombinant proteins formed aggregates resulting in the formation of inclusion bodies. These inclusion bodies must be denatured and refolded to obtain active protein, and the affinity tails are usefiil in the purification of the protein. Some of the methods described herein involve identification of functional domains in proteins (see also Protein engineering). [Pg.247]

Biomedical Applications. TRIS AMINO is used for a number of purposes in its pure form, it is an acidimetric standard the USP grade can be utilized intraveneously for therapeutic control of blood acidosis TRIS AMINO also is useful in genetic engineering as a buffering agent for enzyme systems, industrial protein purification, and electrophoresis. AMP has found use as a reagent in enzyme-linked immunoassays. The primary appHcation is for alkaline phosphatase assays. [Pg.19]

R. K. Scopes, Protein Purification Principles andPractice, 3rd ed., Springer-Vedag, New York, 1994. [Pg.207]

M. P. Deutscher, ed.. Methods in Enymology, Vol.182, Guide to Protein Purification, Academic Press, Inc., San Diego, Calif., 1990. [Pg.207]

E. L. V. Harris and S. Angal, eds.. Protein Purification Methods A Practical Approach, IRL Press at Oxford University Press, Oxford, U.K., 1989. [Pg.207]

Isolation and identification of substances (natural products from nature, protein purification and characterisation, etc). [Pg.72]

Like other GFC matrices, including TSK-GEL SW and TSK-GEL PW packings, and dextran and agarose gels, Toyopearl HW resins exhibit some ionic and hydrophobic interaction with samples. The hydrophobic properties of Toyopearl HW resins, however, can be utilized more effectively for improved protein purifications because, unlike numerous other GFC packing materials, Toyopearl HW resins can be used with high levels of organic solvent (38). [Pg.149]

Example of a Protein Purification Scheme Purification of the Enzyme Xanthine Dehydrogenase from a Eungus... [Pg.130]

Dentscher, M. P., ed., 1990. Guide to Protein Purification. Vol. 182, Methods in Enzymology. San Diego Academic Press, 894 pp. [Pg.152]

Scopes, R. K. (1993). Protein Purification, Principles and Practice, 3rd ed. Springer-Verlag, New York. [Pg.432]


See other pages where Purification protein is mentioned: [Pg.188]    [Pg.20]    [Pg.181]    [Pg.208]    [Pg.279]    [Pg.520]    [Pg.669]    [Pg.821]    [Pg.894]    [Pg.42]    [Pg.47]    [Pg.48]    [Pg.58]    [Pg.58]    [Pg.185]    [Pg.532]    [Pg.200]    [Pg.209]    [Pg.185]    [Pg.2055]    [Pg.2055]    [Pg.2064]    [Pg.503]    [Pg.504]    [Pg.241]    [Pg.247]    [Pg.130]    [Pg.130]    [Pg.392]    [Pg.393]    [Pg.393]   
See also in sourсe #XX -- [ Pg.503 , Pg.562 ]

See also in sourсe #XX -- [ Pg.457 ]

See also in sourсe #XX -- [ Pg.457 ]

See also in sourсe #XX -- [ Pg.503 , Pg.562 ]




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