Laidler P, Gałka-Walczak M, Lityńska A
Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Cracow, Poland.
Acta Biochim Pol. 1995;42(1):45-50.
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.
对来自人胎盘的纯芳基硫酸酯酶B进行等电聚焦分析，结果表明存在高pI（pH 9 - 8）和低pI（pH 6.5 - 5.5）的酶活性和无活性形式。使用聚糖分化试剂盒进行的聚糖链分析表明，人胎盘芳基硫酸酯酶B的碱性形式主要含有高甘露糖/杂合型聚糖，其中6 - O - L - 岩藻糖与最内层的N - 乙酰葡糖胺残基结合，而该酶的酸性形式含有含有岩藻糖和唾液酸的复合型聚糖。然而，后一种形式在总碳水化合物成分中占比很小。对天然酶进行凝集素亲和层析证实存在核心岩藻糖和唾液酸。
