D0292
Bis(3,5-dibromosalicyl) fumarate
≥98% (TLC)
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About This Item
Formula condensata:
C18H8O8Br4
Numero CAS:
Peso molecolare:
671.87
Numero MDL:
Codice UNSPSC:
12352100
ID PubChem:
Saggio
≥98% (TLC)
Stringa SMILE
OC(=O)c1cc(Br)cc(Br)c1OC(=O)\C=C\C(=O)Oc2c(Br)cc(Br)cc2C(O)=O
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
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Lei Huang et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 36(2), 156-165 (2008-04-26)
Hemoglobin-based blood substitute is widely studied. As the starting materials, hemoglobin (Hb) is mainly supplied from outdated human blood and animal sources. But there are many disadvantages. As the alternative source, human placenta hemoglobin (PHb) has its own advantages. We
M S Rogers et al.
Biochimica et biophysica acta, 1248(2), 135-142 (1995-04-27)
Human hemoglobin site specifically cross-linked with bis(3,5-dibromosalicyl)fumarate results in a low oxygen affinity hemoglobin-based red cell substitute (alpha-DBBF). Polymerization of alpha-DBBF by bis(maleoylglycylamide) polyethylene glycol (BMAA-PEG) yields poly alpha-DBBF which offers the added benefits of reduced renal clearance and increased
A I Alayash et al.
Archives of biochemistry and biophysics, 303(2), 332-338 (1993-06-01)
We have examined the interactions between nitric oxide (NO) and oxidized human hemoglobin, comparing the behavior of unmodified HbA0 with that of two chemically modified hemoglobins. The latter are promising red cell substitute candidates due to their lower oxygen affinity
M Samaja et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 22(3), 517-524 (1994-01-01)
The xanthine/xanthine oxidase reaction produces reproducible amounts of oxygen-derived free radicals that oxidize human oxyhemoglobin (Hb). We monitored the kinetics of the oxidation of stripped Hb (sHb), purified HbA0 and alpha-alpha cross-linked Hb (HbXL99 alpha) at [Hb] in the 5
R Motterlini et al.
Artificial cells, blood substitutes, and immobilization biotechnology, 23(3), 291-301 (1995-01-01)
The aim of the present study was to investigate the role of hemoglobin autoxidation in the induction of endothelial heme oxygenase (HO), an inducible "stress" protein which is responsible for heme catabolism. Porcine aortic endothelial cells were incubated for six
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