X3128
Xanthine Agarose
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About This Item
UNSPSC Code:
41106500
NACRES:
NA.56
Productos recomendados
matrix
4% cross-linked agarose
Quality Level
capacity
≥1.5 mg/mL binding capacity (uricase)
storage temp.
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.
signalword
Warning
hcodes
Hazard Classifications
Flam. Liq. 3
Storage Class
3 - Flammable liquids
wgk_germany
WGK 2
flash_point_f
102.9 °F - closed cup
flash_point_c
39.4 °C - closed cup
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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
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)
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
Uricase from leaves: its purification and characterization from three different higher plants.
Montalbini, P., et al.
Planta, 202(3), 277-283 (1997)
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
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