Nagaoka M, Shiraishi T, Furuhata K, Uda Y
Department of Health Chemistry, Niigata College of Pharmacy, Niigata, Japan.
Biol Pharm Bull. 1998 Nov;21(11):1134-8. doi: 10.1248/bpb.21.1134.
The inhibitory effects of various sulfated compounds on the activities of sialidases purified from porcine liver and human placenta were investigated. Among the sulfated compounds tested, heparin, dextran sulfate, condroitin sulfates and sulfatide significantly inhibited the 4-methylumbelliferyl-alpha-N-acetylneuraminic acid (4-MU-NeuAc) sialidase activities of the two enzyme preparations, but glucose 6-sulfate and glucosamine 6-sulfate did not. Potassium sulfate showed an inhibitory effect only at high concentrations. When the sialidase activities were measured using natural substrates, the sialidase activities for the (alpha2-3) and (alpha2-6) sialyllactoses, and colominic acid, were markedly inhibited by heparin and sulfatide similar to 4-MU-NeuAc, although the fetuin sialidase activity was not significantly influenced by them. The sialidase activity hydrolyzing GM3 was strongly inhibited by heparin, but not by sulfatide.
研究了各种硫酸化化合物对从猪肝和人胎盘中纯化的唾液酸酶活性的抑制作用。在所测试的硫酸化化合物中，肝素、硫酸葡聚糖、硫酸软骨素和硫苷脂显著抑制了这两种酶制剂的4-甲基伞形酮基-α-N-乙酰神经氨酸（4-MU-NeuAc）唾液酸酶活性，但6-硫酸葡萄糖和6-硫酸氨基葡萄糖没有。硫酸钾仅在高浓度时显示出抑制作用。当使用天然底物测量唾液酸酶活性时，肝素和硫苷脂对（α2-3）和（α2-6）唾液乳糖以及共聚唾液酸的唾液酸酶活性有显著抑制作用，类似于4-MU-NeuAc，尽管胎球蛋白唾液酸酶活性不受它们的显著影响。水解GM3的唾液酸酶活性受到肝素的强烈抑制，但不受硫苷脂的抑制。
