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Key Documents

D0292

Sigma-Aldrich

Bis(3,5-dibromosalicyl) fumarate

≥98% (TLC)

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About This Item

Linear Formula:
C18H8O8Br4
CAS Number:
Molecular Weight:
671.87
MDL number:
UNSPSC Code:
12352100
PubChem Substance ID:

Assay

≥98% (TLC)

SMILES string

OC(=O)c1cc(Br)cc(Br)c1OC(=O)\C=C\C(=O)Oc2c(Br)cc(Br)cc2C(O)=O

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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Cai Jin et al.
Protein and peptide letters, 11(4), 353-360 (2004-08-26)
Hemoglobin cross-linked with small molecular modifiers turns out to be more stable. Modifications of proteins with polyethylene glycol (PEG) have been proven to enlarge the molecular size of proteins, to prolong their retention time in the circulation as well as
Y Osawa et al.
Biochemical pharmacology, 46(12), 2299-2305 (1993-12-14)
One approach to the development of an effective red cell substitute has been chemical modification of human hemoglobin to optimize oxygen transport and plasma half-life. Human hemoglobin A0 and two of these modified hemoglobins, one prepared from the cross-linking of
Z Yu et al.
Protein science : a publication of the Protein Society, 6(12), 2568-2577 (1998-01-07)
Diaspirin crosslinked hemoglobin (DCLHb) was analyzed by mass spectrometric-based techniques to identify the protein modifications effected by the crosslinking reaction with bis(3,5-dibromosalicyl) fumarate. DCLHb consists of two principal components. These components were isolated by size-exclusion chromatography and identified by measurement
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
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

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