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

• Autorzy: Laidler P. , Galka-Walczak M. , Litynska A.
• Języki publikacji: EN

Abstrakty

EN

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.

Słowa kluczowe

EN

arylosulphatase B; oligosaccharide; human placenta; lectin binding

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 1995
• Tom: 42
• Numer: 1
• Opis fizyczny: p.45-50,fig.

Twórcy

autor

Laidler P.

• Collegium Medicum, Jagiellonian University, M.Kopernika 7, 31-034 Cracow, Poland

autor

Galka-Walczak M.

autor

Litynska A.

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