Preliminary characterization of the oligosaccharide component of arylsulfatase B from human placenta
Laidler, P.; Gałka-Walczak, M.; Lityńska, A.
Acta Biochimica Polonica 42(1): 45-50
1995
ISSN/ISBN: 0001-527X PMID: 7653160 Document Number: 444444
Isoelectric focusing of homogenous arylsulfatase B from human placenta pointed to the presence of enzymatically active and inactive forms of high pI (pH 9-8) and of lower pI (pH 6.5-5.5). Glycan chain analysis performed with the use of a Glycan Differentiation Kit showed that basic forms of arylsulfatase B from human placenta contained mostly high mannose/hybrid type glycans, with 6-O-L-fucose bound to the innermost N-acetylglucosamine residue, whereas acidic forms of the enzyme contained complex type glycans containing fucose and sialic acid. However, the latter forms constitute a small percentage of the total carbohydrate component. Lectin affinity chromatography of the native enzyme confirmed the presence of a core fucose and a sialic acid.