CHEMICAL CHARACTERIZATION OF AN IMMUNOSUPPRESSIVE GLYCOPROTEIN

尿调节蛋白赖氨酰残基的琥珀酰化导致尿调节蛋白的解折叠。 糖蛋白的二级结构，但不干扰 尿糖蛋白抑制免疫反应的能力。 赖氨酰残基的三硝基苯化不影响结构， 它会影响免疫抑制特性 酪氨酰的修饰 通过碘化、硝化或O-乙酰化的残基不影响 尿调节素抑制淋巴细胞增殖的能力。 实际上 似乎尿调节蛋白的蛋白质部分在 抑制免疫反应 该活动似乎位于 寡糖部分。

Succinylation of lysyl residues of uromodulin results in the unfolding of the secondary structure of the glycoprotein but does not interfere with the ability of the urinary glycoprotein to suppress the immune response. Trinitrophenylation of lysyl residue does not affect the structure nor does it affect the immunosuppressive properties. Modification of tyrosyl residues by iodination, nitration or O-acetylation does not affect the ability of uromodulin to suppress lymphocyte proliferation. In fact, it appears that the protein moiety of uromodulin plays a minor role in suppressing the immune response. The activity appears to reside in the oligosaccharide moiety.