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目的探讨人类β1,3N-乙酰氨基葡萄糖基转移酶8/β3半乳糖基转移酶7(β3GnT8/β3GalT7)与人4IgB7-H3蛋白的相互作用,以期阐明该糖基转移酶对人4IgB7-H3蛋白的翻译后糖基化修饰作用。方法在线预测软件预测人4IgB7-H3蛋白氨基酸序列上潜在的糖基转移酶作用位点;免疫共沉淀探讨β3GnT8/β3GalT7与人4IgB7-H3蛋白的相互结合作用;细胞免疫荧光化学技术研究两种蛋白质在细胞内的空间定位。结果人4IgB7-H3蛋白氨基酸序列上潜在的N-糖基化位点共有8个,O-β-GlcNAc的附着位置共有18个;β3GnT8/β3GalT7与人4IgB7-H3蛋白能相互结合而被共沉淀;两种蛋白质能在人肺癌A549细胞中共定位。结论人类β3GnT8/β3GalT7可能对人4IgB7-H3蛋白有糖基化修饰作用。
Objective To investigate the interaction of humanβ1,3-N-acetylglucosaminyltransferase8 / β3galactosyltransferase7 (β3GnT8 / β3GalT7) with human4IgB7-H3protein in order to elucidate the effect of this glycosyltransferase on human4IgB7-H3 protein Posttranslational glycosylation modification. Methods Online prediction software was used to predict the potential glycosyltransferase sites in the amino acid sequence of human 4IgB7-H3 protein. Co-immunoprecipitation was used to investigate the interaction between β3GnT8 / β3GalT7 and human 4IgB7-H3 protein. Immunocytochemistry Positioning within the cell’s space. Results There were 8 potential N-glycosylation sites in the amino acid sequence of human 4IgB7-H3 protein and 18 sites of O-β-GlcNAc. The β3GnT8 / β3GalT7 and human 4IgB7-H3 proteins could be coprecipitated Both proteins can colocalize in human lung cancer A549 cells. Conclusion Human β3GnT8 / β3GalT7 may be glycosylated on human 4IgB7-H3 protein.