Preliminary characterization of the oligosaccharide component of arylsulfatase B from human placenta.
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.
Laidler
P
P
Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Cracow, Poland.
Gałka-Walczak
M
M
Lityńska
A
A
D002803:Chondro-4-Sulfatase / Q000737:chemistry*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D005260:Female; D005643:Fucose / Q000302:isolation & purification; D006801:Humans; D007525:Isoelectric Focusing; D037102:Lectins / Q000378:metabolism; D008358:Mannose / Q000302:isolation & purification; D019158:N-Acetylneuraminic Acid; D009844:Oligosaccharides / Q000737:chemistry*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D012794:Sialic Acids / Q000302:isolation & purification
D037102:Lectins; D009844:Oligosaccharides; D012794:Sialic Acids; D005643:Fucose; D002803:Chondro-4-Sulfatase; D019158:N-Acetylneuraminic Acid; D008358:Mannose