Di Natale P, Ronsisvalle L
Biochim Biophys Acta. 1981 Sep 15;661(1):106-11. doi: 10.1016/0005-2744(81)90088-7.
Iduronate sulfatase of human placenta separates on DEAE Bio-Gel A chromatography into two components, a less acidic form A and a more acidic form B. The two forms have different mobilities on gel electrophoresis and different isoelectric points, pH 5.0 for form A and pH 4.5 for form B. They show the same pH optima in sodium acetate buffer and similar Km values for [3H]disulfated disaccharide substrate. Iduronate sulfatase A is more heat labile than iduronate sulfatase B. Different molecular weights were found by gel filtration while similar values were estimated by sucrose gradient centrifugation. Neuraminidase treatment of the two forms gives evidence that these enzymes contain sialic acid residues.
人胎盘艾杜糖醛酸硫酸酯酶经二乙氨基乙基琼脂糖凝胶A柱层析可分离成两个组分，酸性较弱的A形式和酸性较强的B形式。这两种形式在凝胶电泳中的迁移率不同，等电点也不同，A形式的pH值为5.0，B形式的pH值为4.5。它们在醋酸钠缓冲液中表现出相同的最适pH值，对[3H]二硫酸化二糖底物的Km值相似。艾杜糖醛酸硫酸酯酶A比艾杜糖醛酸硫酸酯酶B更不耐热。通过凝胶过滤发现分子量不同，而通过蔗糖梯度离心估计的值相似。对这两种形式进行神经氨酸酶处理表明这些酶含有唾液酸残基。
