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采用固相结合试验证实:(1)rTNF-α和 rIL-2能以高度亲和力与多种含 N-连接寡糖的糖蛋白结合,其结合活性依赖于糖蛋白的糖基组分;(2)rTNF-α能识别各种类型的 N-连接糖链,而 rIL-2只能与高甘露糖型的 N-连接糖链结合;(3)甘露三糖特导地抑制 rTNF-α和 rIL-2与糖蛋白的结合;(4)rTNF-α和 rIL-2不能识别 O-连接的寡糖,由此表明,TNF 和 IL-2均为对 N-连接寡糖特异的凝集素,它们特异性识别的碳水化合物部位可能是 N-连接寡糖的核心结构.鉴于 N-连接的寡糖广泛存在于人类的分泌蛋白和膜糖蛋白,故单核,淋巴因子的碳水化合物结合活性在人类免疫反应调节中的作用将是一个值得探索的新领域.
The solid-phase binding assay confirmed that: (1) rTNF-α and rIL-2 can bind to a variety of N-linked oligosaccharide-containing glycoproteins with high affinity and their binding activity depends on the glycosyl component of glycoprotein; (2 ) rTNF-α recognizes various types of N-linked sugar chains, whereas rIL-2 binds only to N-linked sugar chains of high mannose type; (3) Mannotriose specifically inhibits both rTNF-α and rIL -2 and glycoprotein; (4) rTNF-α and rIL-2 do not recognize O-linked oligosaccharides, thus indicating that both TNF and IL-2 are lectins specific for N-linked oligosaccharides and that they Specific recognition of carbohydrate sites may be the core structure of N-linked oligosaccharides Given the widespread presence of N-linked oligosaccharides in human secreted proteins and membrane glycoproteins, monokaryotic, lymphokine carbohydrate-binding activity in humans The role of immune response regulation will be a new area worth exploring.