Structural analysis of N-glycans from human neutrophil azurocidin.
N-glycans of human neutrophil azurocidin, enzymatic inactive homolog of serine proteinase playing important and multifunctional roles in antimicrobial defense, endotoxin binding, monocyte, and T-cell activation, were isolated by hydrazinolysis and fluorescence labeled. An ion-exchange chromatography on GlycoSep C column separated neutral, mono-, and disialylated glycans. The glycans from each group were separated subsequently on GlycoSep N and GlycoSep H columns. Sequential exoglycosidase treatment and HPLC mapping allowed determining 21 different glycan structures, majority of them being neutral (79.8%), the rest-mono- (13.1%) and disialylated (1.2%).
Olczak
Mariusz
M
Institute of Biochemistry and Molecular Biology, Wrocław University, Tamka 2, 50-137 Wrocław, Poland.
Watorek
Wiesław
W
D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins / Q000737:chemistry* / Q000302:isolation & purification; D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002352:Carrier Proteins / Q000737:chemistry* / Q000302:isolation & purification; D006023:Glycoproteins / Q000737:chemistry; D006026:Glycoside Hydrolases; D006801:Humans; D008969:Molecular Sequence Data; D009504:Neutrophils; D009844:Oligosaccharides / Q000737:chemistry* / Q000302:isolation & purification; D011134:Polysaccharides / Q000737:chemistry* / Q000302:isolation & purification
C062991:AZU1 protein, human; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D006023:Glycoproteins; D009844:Oligosaccharides; D011134:Polysaccharides; D006026:Glycoside Hydrolases