Slomiany B L, Murty V L, Piotrowski J, Liau Y H, Sundaram P, Slomiany A
Research Center, New Jersey Dental School, University of Medicine and Dentistry of New Jersey, Newark 07103-2400.
Biochem Biophys Res Commun. 1992 Mar 16;183(2):506-13. doi: 10.1016/0006-291x(92)90511-i.
A glycosulfatase activity toward sulfated gastric mucus glycoprotein was identified in the extracellular material elaborated by H. pylori, a bacteria implicated in the etiology of gastric disease. Upon acetone precipitation, an active enzyme fraction at 64% acetone was obtained which on SDS-PAGE gave a major 30kDa protein band. The H. pylori glycosulfatase exhibited maximum activity (314.8 pmol/mg protein/h) at pH 5.7 in the presence of Triton X-100 and CaCl2, and was capable of removal of the sulfate ester groups situated at C-6 of N-acetylglucosamine, galactose and glucose. However, the enzyme was ineffective toward galactosylceramide and lactosylceramide sulfates which contain the sulfate ester group on C-3 of galactose. The results suggest that H. pylori is capable of overcoming the interference by sulfated mucus glycoprotein with its colonization of gastric mucosa.
在由幽门螺杆菌（一种与胃部疾病病因有关的细菌）产生的细胞外物质中，发现了一种针对硫酸化胃黏液糖蛋白的糖硫酸酯酶活性。经丙酮沉淀后，获得了在64%丙酮浓度下的活性酶组分，该组分在SDS - PAGE上呈现出一条主要的30kDa蛋白条带。幽门螺杆菌糖硫酸酯酶在pH 5.7、存在Triton X - 100和CaCl2的条件下表现出最大活性（314.8 pmol/mg蛋白/小时），并且能够去除位于N - 乙酰葡糖胺、半乳糖和葡萄糖C - 6位的硫酸酯基团。然而，该酶对在半乳糖C - 3位含有硫酸酯基团的半乳糖神经酰胺和乳糖神经酰胺硫酸盐没有作用。结果表明，幽门螺杆菌能够克服硫酸化黏液糖蛋白对其在胃黏膜定植的干扰。
