X3128
Xanthine Agarose
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About This Item
Code UNSPSC :
41106500
Nomenclature NACRES :
NA.56
Produits recommandés
Matrice
4% cross-linked agarose
Capacité
≥1.5 mg/mL binding capacity (uricase)
Température de stockage
2-8°C
Application
Xanthine-agarose is used for protein chromatography, affinity chromatography and specialty resins. Xanthine-agarose has been used to purify and determine molecular properties of urate oxidase from Chlamydomonas reinhardtii. Xanthine-agarose has also been used to determine physicochemical properties and states of sulfhydryl groups of uricase from Candida utilis.
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Flam. Liq. 3
Code de la classe de stockage
3 - Flammable liquids
Classe de danger pour l'eau (WGK)
WGK 2
Point d'éclair (°F)
102.9 °F - closed cup
Point d'éclair (°C)
39.4 °C - closed cup
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Les clients ont également consulté
S S Mösli Waldhauser et al.
Phytochemistry, 45(7), 1407-1414 (1997-08-01)
Caffeine biosynthesis comprises sequential methylations at N-7, N-3 and N-1 of the xanthine ring catalysed by S-adenosyl-L-methionine (SAM)-dependent methyltransferase activities that, to date, have not been resolved. Enzyme extracts were prepared from young, emerging coffee leaflets and following anion exchange
J M Alamillo et al.
Biochimica et biophysica acta, 1076(2), 203-208 (1991-01-29)
Urate oxidase (urate: oxygen oxidoreductase, EC 1.7.3.3) from the unicellular green alga Chlamydomonas reinhardtii has been purified to electrophoretic and immunological homogeneity by a procedure which includes as main steps ammonium sulfate fractionation, gel filtration, ion exchange and xanthine-agarose affinity
H Nishimura et al.
Journal of biochemistry, 91(1), 41-48 (1982-01-01)
Highly purified uricase [urate: oxygen oxidoreductase, EC 1.7.3.3] was obtained from Candida utilis by affinity chromatography with xanthine-agarose conjugate followed by chromatography with Sephadex G-200 in the presence of dithiothreitol. The uricase molecule had a molecular weight of 120,000 and
Débora da Silva Freitas et al.
International journal of pharmaceutics, 387(1-2), 215-222 (2009-12-09)
PEGylation is a successful strategy for improving the biochemical and biopharmaceutical properties of proteins and peptides through the covalent attachment of polyethylene glycol chains. In this work, purified recombinant uricase from Candida sp. (UC-r) was modified by PEGylation with metoxypolyethilenoglycol-p-nitrophenyl-carbonate
Isolation and characterization of uricase from bean leaves and its comparison with uredospore enzymes.
Montalbini, P., et al.
Plant Science, 147(2), 139-147 (1999)
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