A5926
N-Acetyl-D-galactosamine 4-sulfate, sodium salt, mixed anomers
≥98%
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About This Item
Linear Formula:
C8H14O9NSNa
CAS Number:
Molecular Weight:
323.25
MDL number:
UNSPSC Code:
12352201
PubChem Substance ID:
assay
≥98%
storage temp.
−20°C
SMILES string
[Na].CC(=O)NC(C=O)C(O)C(OS(O)(=O)=O)C(O)CO
Application
N-Acetyl-D-galactosamine 4-sulfate (GalNAc-4S) is used as a substrate to identify, differentiate and characterize N-acetylgalactosamine sulfatase(s) and arylsulfatase(s).
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Development of a functional bioassay for arylsulfatase B using the natural substrates of the enzyme.
Erno Pungor et al.
Analytical biochemistry, 395(2), 144-150 (2009-08-18)
A functional bioassay has been developed for measuring the intracellular activity of recombinant human arylsulfatase B (rhASB) on its natural glycosaminoglycan (GAG) substrates, dermatan sulfate (DS), and chondroitin sulfate (CS) when the enzyme is taken up into cultured ASB-deficient human
M Masue et al.
Journal of biochemistry, 110(6), 965-970 (1991-12-01)
N-Acetylgalactosamine-6-sulfate sulfatase from human placenta was purified 33,600-fold using beta-N-acetyl-D-galactosamine 6-sulfate-(1----4)-beta-D-glucuronic acid-(1----3)-N-acetyl-D-[3H]galactosaminitol 6-sulfate as the substrate. This enzyme is an oligomer with a molecular mass of 120 kDa and consists of polypeptides of 40 and 15 kDa. The 15 kDa
G J Gibson et al.
The Biochemical journal, 248(3), 755-764 (1987-12-15)
Initial purification of N-acetylgalactosamine-4-sulphate sulphatase from human liver homogenates containing approx. 1 mg of enzyme in 26 g of soluble proteins was achieved by a six-column chromatography procedure and yielded approx. 40 micrograms of a single major protein species. Enzyme
J Bielicki et al.
The Biochemical journal, 279 ( Pt 2), 515-520 (1991-10-15)
Human N-acetylgalactosamine 6-sulphatase (EC 3.1.6.14), which is involved in the lysosomal degradation of the glycosaminoglycans keratan sulphate and chondroitin 6-sulphate, was purified more than 130,000-fold in 2.8% yield from liver by an eight-step column procedure. One major form was identified
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