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

Abstract:

: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.

journal_name

Acta Biochim Pol

journal_title

Acta biochimica Polonica

authors

Laidler P,Gałka-Walczak M,Lityńska A

subject

Has Abstract

pub_date

1995-01-01 00:00:00

pages

45-50

issue

1

eissn

0001-527X

issn

1734-154X

journal_volume

42

pub_type

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