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D-Galactose-4-sulfat Natriumsalz
≥97.0% (TLC)
Synonym(e):
Gal-4S
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About This Item
Lineare Formel:
C6H11O9SNa
CAS-Nummer:
Molekulargewicht:
282.20
MDL-Nummer:
UNSPSC-Code:
12352201
PubChem Substanz-ID:
NACRES:
NA.25
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Assay
≥97.0% (TLC)
Lagertemp.
−20°C
SMILES String
[Na+].OC[C@@H](O)[C@H](OS([O-])(=O)=O)[C@H](O)[C@@H](O)C=O
InChI
1S/C6H12O9S.Na/c7-1-3(9)5(11)6(4(10)2-8)15-16(12,13)14;/h1,3-6,8-11H,2H2,(H,12,13,14);/q;+1/p-1/t3-,4+,5+,6-;/m0./s1
InChIKey
PPFRJSVPFMKACS-NQZVPSPJSA-M
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Anwendung
D-Galactose 4-sulfate (Gal-4S) may be used to help differentiate glycan sulfatide recognition/binding sites and to study the structure and biochemisty of carrageenans.
Verpackung
Bottomless glass bottle. Contents are inside inserted fused cone.
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Rando Tuvikene et al.
Carbohydrate research, 344(6), 788-794 (2009-03-10)
The composition, structure, and thermal stability of carrageenans from unattached Coccotylus truncatus (the Baltic Sea, Estonia) were investigated. The complex polysaccharide was characterized by (13)C NMR and FTIR spectroscopy, ICP-OES and gel permeation chromatography methods. The main components of C.
S Yamada et al.
European journal of biochemistry, 233(2), 687-693 (1995-10-15)
The carbohydrate-protein linkage region of a chondroitin 4-sulfate chain attached to urinary trypsin inhibitor (UTI) was isolated from human urine and characterized structurally. The chondroitin 4-sulfate chain was released from UTI by beta-elimination using alkaline NaBH4 then digested with chondroitinase
T Barbeyron et al.
The Journal of biological chemistry, 275(45), 35499-35505 (2000-08-10)
iota-Carrageenases are polysaccharide hydrolases that cleave the beta-1,4 linkages between the d-galactose-4-sulfate and 3, 6-anhydro-d-galactose-2-sulfate residues in the red algal galactans known as iota-carrageenans. We report here on the purification of iota-carrageenase activity from the marine bacterium Zobellia galactanovorans and
Lena Jansson et al.
PloS one, 4(2), e4487-e4487 (2009-02-27)
The first step in the pathogenesis of enterotoxigenic Escherichia coli (ETEC) infections is adhesion of the bacterium to the small intestinal epithelium. Adhesion of ETEC is mediated by a number of antigenically distinct colonization factors, and among these, one of
Astrid Von Mentzer et al.
Virulence, 11(1), 381-390 (2020-04-05)
The ability to adhere via colonization factors to specific receptors located on the intestinal mucosa is a key virulence factor in enterotoxigenic Escherichia coli (ETEC) pathogenesis. Here, the potential glycosphingolipid receptors of the novel human ETEC colonization factor CS30 were
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