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Preliminary characterization of the oligosaccharide component of arylsulfatase B from human placenta

100%

Laidler P., Galka-Walczak M., Litynska A.

Acta Biochimica Polonica

1995

tom 42

nr 1

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 AT-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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Galka-Walczak M.

1 Laidler P.

1 Litynska A.

1 1995

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Preliminary characterization of the oligosaccharide component of arylsulfatase B from human placenta