Bioaffinity chromatography

Other chromatographic methods should also be mentioned gel-permeation methods (molecular sieving), car-boxymethyl (CM) cellulose chromatography, bioaffinity... 

In addition to the covalent binding, some methods derived from bioaffinity chromatography can be used for non covalent attachment of antibodies to a surface by the inactive Fc portion. The advantage is that antigen binding sites stay undamaged and accessible for the analytes due to the orientation of antibody with the active Fab portions towards the tested medium. 

Bioaffinity chromatography, 6 399—400 Bioantimutagen, vanillin as, 25 556 Bioassay dyes, 9 518 Bioassays, microfluidics in, 26 968-969 Bioaugmentation, defined, 3 758t Bioaugmentation/bioremediation effluent treatment, 9 436, 438 Bioavailability, of antisense oligonucleotides, 17 628 Biocatalysis, 3 668-683 16 395. See also Biocatalyst entries... 

PORATH, J. J. Chrom. 218 (1981) 241. Development of modem bioaffinity chromatography. 

The earliest applications of bioaffinity chromatography involved its use in enzyme purification (see Figure 13.7) [7]. Enzyme purification has continued to be a major application of this technique [57]. Some ligands that are employed for this purpose are enzyme inhibitors, coenzymes, substrates, and cofactors. Examples include methods that use nucleotide mono-, di-, and triphosphates for the... 

Immunoaffinity chromatography is probably the most highly specific of all forms of bioaffinity chromatography. However this technique has some disadvantages such as this technique relatively high cost, leakage of ligands may accur from the column and sometimes the desorption procedure results in partial denaturation of the bound protein [24]. 

Enz)mies, inhibitors, cofactors, nucleic acids, hormones or cell chromatography can also be utilized as ligands in bioaffinity chromatography types. Examples of these methods include Receptor Affinity Chromatography and DNA Affinity Chromatography [21]. 

Both Parts I and II have been completely rewritten and reflect the many advances in biochemistry-molecular biology theory and techniques. Especially noteworthy have been the technical advances in chromatography (perfusion, FPLC, bioaffinity), electrophoresis (pulsed gel, capillary, nucleic acid sequencing), spectrophotometry (nmr, ms, and diode array detectors), and molecular biology (microsequencing of proteins and nucleic acids, blotting, restriction enzymes). 

Metal chelate and bioaffinity chromatography based on the affinity of the protein for a specific molecule that can be incorporated in the stationary phase (not commonly used for food analysis)... 

Figure 6.10 Procedure for bioaffinity screening of combinatorial drug candidates libraries with two cycles of iterative size exclusion chromatography, using spin columns to separate the receptor and receptor-binder complexes from unbound ligands. (Reprinted with permission from Davis et al., 1999. Copyright 1999 American Chemical Society.)...

Yoshida, K. Takegami, T. Isolation of cytokinin binding protein from tobacco leaves by bioaffinity chromatography and its partial characterization. J. Biochem., 1977, 81, 791-799. 

Volume 55 Bioaffinity Chromatography. Second, completely revised edition by J. Turkova... 

J. Turkova, M. Fusek, J. J. Maksimov, and Y. B. Alakholv, Int. Symp. Bioaffinity-Chromatography. Retat. Techn. Abstr. L26. 

Figure 13.11. Bioaffinity electrospray FTICR mass spectrometry. The isolation and mass spectrometricidentificationof receptor-specific ligands are carried out entirely in the mass spectrometer without chromatography or other separation steps.

The kinetics of adsorption-desorption is rarely slow in preparative chromatography, and most examples of a slow kinetics are foimd in bioaffinity chromatography, or in the separation of proteins. Thus, there are few cases in which a reaction-kinetic model is appropriate. This model is important, however, because there are many cases where it is convenient to model the finite rate of the mass transfer... 

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