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
Uricase from leaves: its purification and characterization from three different higher plants.
Montalbini, P., et al.
Planta, 202(3), 277-283 (1997)
Marialaura Marchetti et al.
Scientific reports, 6, 38302-38302 (2016-12-07)
Urate oxidase (Uox) catalyses the first reaction of oxidative uricolysis, a three-step enzymatic pathway that allows some animals to eliminate purine nitrogen through a water-soluble compound. Inactivation of the pathway in hominoids leads to elevated levels of sparingly soluble urate
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)
Miguel Aguilar et al.
Current microbiology, 44(4), 257-261 (2002-03-23)
Uricase (urate: oxygen oxidoreductase; EC 1.7.3.3) from the rust Puccinia recondita was purified to electrophoretic homogeneity. Preparations with a specific activity of 8.4 U/mg were used for characterization of the enzyme, which showed a strong similarity to other plant and
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
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