Zanetta J P, Reeber A, Dontenwill M, Vincendon G
J Neurochem. 1984 Feb;42(2):334-9. doi: 10.1111/j.1471-4159.1984.tb02683.x.
Two different methods were set up to detect the possible presence of lectin-like molecules with a specificity for mannose-rich glycans in the rat cerebellum. The first, affinity histochemistry, involved the isolation of a particular class of glycoproteins from the cerebella of 11-day-old rats followed by the formation of covalent complexes with horseradish peroxidase and then incubation with cerebellar slices. The second used in vitro interactions between [3H]leucine-labeled proteins, kept in solution, with insolubilized [14C]glucosamine-labeled glycoproteins. The results of both methods are compatible with the presence of lectin-like activities inhibited by high mannose concentrations, but not other sugars. However, the binding sites preferred by these molecules seem to be more than a single mannose residue.
建立了两种不同的方法来检测大鼠小脑中可能存在的对富含甘露糖聚糖具有特异性的凝集素样分子。第一种方法是亲和组织化学，从11日龄大鼠的小脑中分离出一类特定的糖蛋白，然后与辣根过氧化物酶形成共价复合物，再与小脑切片一起孵育。第二种方法是利用溶解状态下的[3H]亮氨酸标记蛋白与不溶性[14C]葡萄糖胺标记糖蛋白之间的体外相互作用。两种方法的结果均表明存在被高浓度甘露糖抑制但不被其他糖类抑制的凝集素样活性。然而，这些分子偏好的结合位点似乎不止一个甘露糖残基。
