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Steady state kinetic analysis of O-linked GalNAc glycan release catalyzed by endo-α-N-acetylgalactosaminidase
Dennis K. Hansen,
Jakob R. Winther
,
Martin Willemoës
Department of Biology
Biomolecular Sciences
1
Citation (Scopus)
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Medicine & Life Sciences
Bifidobacterium longum
11%
caseinomacropeptide
13%
Cattle
6%
endo-alpha-sialidase
100%
Enzymes
12%
Glycoconjugates
19%
Glycopeptides
38%
Glycoproteins
13%
Glycoside Hydrolases
9%
Glycosides
9%
Kinetics
38%
N-Acetylneuraminic Acid
8%
Neuraminidase
8%
Peptides
4%
Polysaccharides
50%
Proteins
2%
Thomsen-Friedenreich antigen
12%
Chemical Compounds
Chromophore
11%
Cleavage
9%
Enzyme Activity
11%
Glycopeptide
60%
Glycoprotein
24%
Glycoside
12%
Heterogeneity
12%
Molecule
4%
Peptide
7%
Pharmacokinetics
30%
Reaction Stoichiometry
10%
Sialic Acid
14%