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Affinity chromatography matrix

Malmstadt, N., Yager, R, Hoffman, A.S., Stayton, P.S., A smart microfluidic affinity chromatography matrix composed of poly(n-isopropylacrylamide)-coated beads. Anal. Chem. 2003, 75, 2943-2949. [Pg.414]

The lectin from Ricinus communis coupled to Sepharose 4B has been used as an affinity-chromatography matrix in the purification of glycoproteins containing terminal D-galactosyl residues. ... [Pg.323]

Cyclohexa-amylose reacted with an epoxy derivative of agarose to yield an affinity-chromatography matrix that is suitable for use in the purification of j -amylase. ... [Pg.464]

Affinity chromatography, which is the binding of bio-molecules with the matrix bed, often used for antibodies and antigens... [Pg.188]

The fact that adenosine and its derivatives are azo coupling components is used for immobilizing nicotinamide-adenine nucleotide (NAD+) for affinity chromatography purposes. In 12.58 NAD+ is bonded to a matrix through an azo bond. Compound 12.58 is used for the purification of dehydrogenase enzymes (Hocking and Harris, 1973). [Pg.328]

Patwardhan, A.V. and Ataai, M.M., Site accessibility and the pH dependence of the saturation capacity of a highly cross-linked matrix. Immobilized metal affinity chromatography of bovine serum albumin on Chelating Superose, /. Chromatogr. A, 767, 11, 1997. [Pg.137]

Metal-chelate affinity chromatography is a powerful purification technique whereby proteins or other molecules can be separated based upon their ability to form coordination complexes with immobilized metal ions (Porath et al., 1975 Lonnerdal and Keen, 1982 Porath and Belew, 1983 Porath and Olin, 1983 Sulkowski, 1985 Kagedal, 1989). The metal ions are stabilized on a matrix through the use of chelating compounds which usually have multivalent points of interaction with the metal atoms. To form useful affinity supports, these metal ion complexes must have some free or weakly associated and exchangeable coordination sites. These exchangeable sites then can form complexes with coordination sites on proteins or other molecules. Substances that are able to interact with the immobilized metals will bind and be retained on... [Pg.814]

Bethell, G.S., Ayers, J.S., Hancock, W.S., and Hearn, M.T.W. (1979) A novel method of activation of cross-linked agaroses with l,l -carbonyldiimidazole which gives a matrix for affinity chromatography devoid of additional charged groups./. Biol. Chem. 254, 2572-2574. [Pg.1047]

Figure 6.14 Schematic representation of the principle of biospecific affinity chromatography. The chosen affinity ligand is chemically attached to the support matrix (agarose bead) via a suitable spacer arm. Only those ligands in solution that exhibit biospecific affinity for the immobilized species will be retained... Figure 6.14 Schematic representation of the principle of biospecific affinity chromatography. The chosen affinity ligand is chemically attached to the support matrix (agarose bead) via a suitable spacer arm. Only those ligands in solution that exhibit biospecific affinity for the immobilized species will be retained...
The principles of enzyme immobilization on solid phases and the requirements for such solid phases are in general the same as those applied for sorbents and protein ligands used in affinity chromatography. Some time ago the main requirements for the ideal matrix were formulated as follows [84] ... [Pg.175]

Furthmayr, H. (1982). Immunization procedures, isolation by affinity chromatography and seriological and immunochemical characterization of collagen-specific antibodies. In Furthmayr, H., ed. immunochemistry of the Extracellular Matrix, Vol. 1. CRC Press, Boca Raton, FL. [Pg.154]


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See also in sourсe #XX -- [ Pg.238 , Pg.239 ]




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Affinity chromatography

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