Suiko M, Liu M C
Miyazaki University, Japan.
Biochem Biophys Res Commun. 1988 Aug 15;154(3):1094-8. doi: 10.1016/0006-291x(88)90253-7.
Desulfated form of the 3Y1 secreted fibronectin was prepared by treatment with arylsulfatases. Under optimal conditions, the degrees of tyrosine-desulfation of [35S]sulfate-labeled fibronectin by arylsulfatases from Helix pomatia (Type H-1), Patalle vulgata (Type V) and Abalone entrails (Type VIII) were determined to be 55.7%, 54.9% and 76.4%. Upon desulfation of [3H]leucine-labeled fibronectin by Type H-1 or Type V arylsulfatase, gelatin-binding affinity remained unchanged; while heparin-binding affinity increased nearly 50%. Treatment with Type VIII arylsulfatase caused a considerable decrease in gelatin-binding and a slight decrease in heparin-binding affinities. Nevertheless, desulfation by all three enzymes consistently resulted in a dramatic decrease of fibrin-binding affinity, ranging from 42.1% to 64.4%.
3Y1分泌型纤连蛋白的去硫酸化形式是通过用芳基硫酸酯酶处理制备的。在最佳条件下，测定了来自苹果螺（H-1型）、普通滨螺（V型）和鲍鱼内脏（VIII型）的芳基硫酸酯酶对[35S]硫酸盐标记的纤连蛋白的酪氨酸去硫酸化程度分别为55.7%、54.9%和76.4%。用H-1型或V型芳基硫酸酯酶对[3H]亮氨酸标记的纤连蛋白进行去硫酸化后，其与明胶的结合亲和力保持不变；而与肝素的结合亲和力增加了近50%。用VIII型芳基硫酸酯酶处理导致与明胶的结合显著降低，与肝素的结合亲和力略有降低。然而，这三种酶的去硫酸化均导致与纤维蛋白的结合亲和力显著下降，下降幅度在42.1%至64.4%之间。
