Affinity chromatographic method enzymes

Immobilized enzymes may be used in affinity chromatographic methods but their use as catalysts may be in either the production or removal of compounds in chemical processes or as analytical tools. Many substrate assays can be performed using enzymes immobilized on a variety of surfaces, e.g. glass beads, plastic or nylon tubing. Alternatively they may be incorporated into gel or microparticulate layers on dry strips or slides. 

An Affinity Chromatographic Method for the Purification of Some Cellulolytic Enzymes... 

A major advance in the elimination of catalytic site inhomogeneity in new preparations came with the development of an affinity chromatographic method (65) for purifying the enzyme. This method made use of the known high affinity of xanthine oxidase for alloxanthine when the enzyme is in a fully reduced state. By attaching alloxanthine to a polymeric matrix, a selective absorption of active enzyme was achieved. 

An affinity chromatographic method developed for the purification of a-L-fucosidase I from almond emulsin was based on modified agarose derivatized with 6-aminohexanoyl-lacto-A-fucopentaosylamine. The final enzyme preparation was free from other glycoside hydrolases. 

Reverse transcriptase (from avian or murine RNA tumour viruses) [9068-38-6] [EC 2.7.7.49]. Purified by solubilising the virus with non-ionic detergent. Lysed virions were adsorbed on DEAE-cellulose or DEAE-Sephadex columns and the enzyme eluted with a salt gradient, then chromatographed on a phosphocellulose column and enzyme activity eluted in a salt gradient. Purified from other viral proteins by affinity chromatography on a pyran-Sepharose column. [Verna Biochim Biophys Acta 473 1 7977 Smith Methods Enzymol 65 560 1980 see commercial catalogues for other transcriptases.]... 

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