CARBOHYDRATE CHARACTERIZATION OF PURIFIED THYROXINE-BINDING GLOBULIN BY LECTIN BLOT AND ISOELECTRIC FOCUSING

M. Petrovic, B. S. Savin-Zegarac, I. Baričević, S. Cvejic
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引用次数: 1

Abstract

Summary: The structure of carbohydrate moiety of purified thyroxine-binding globulin (TBG) was examined by lectin blot and isoelectric focusing (IEF). In lectin blot, TBG reacted positively with the following lectins: Sambucus nigra agglutinin (SNA I), Ricinus communis agglutinin (RCA I), wheat germ lectin (WGA), phytoheamagglutinin (PHA) and pea lectin (PSA). The obtained results indicate that purified TBG contains N-linked oligosaccharide chains consisting of mannose, galactose, N-acetylglucosamine and sialic acid. Isoelectric focusing of TBG at pI 4.2’ 4.6 revealed three bands, which confirmed that isolated TBG had retained its structure without desialylation. Lectin blot analysis and IEF can be considered to be useful tools in the study of TBG glycosylation.
凝集素印迹和等电聚焦技术对纯化甲状腺素结合球蛋白的碳水化合物特性研究
摘要:采用凝集素印迹和等电聚焦(IEF)技术对纯化的甲状腺素结合球蛋白(TBG)的碳水化合物部分结构进行了研究。在凝集素印迹实验中,TBG与黑参凝集素(SNA I)、蓖麻凝集素(RCA I)、小麦胚芽凝集素(WGA)、植物血凝素(PHA)和豌豆凝集素(PSA)均呈阳性反应。结果表明,纯化后的TBG含有由甘露糖、半乳糖、n -乙酰氨基葡萄糖和唾液酸组成的n -连锁低聚糖链。在pI为4.2’4.6的等电聚焦下,TBG显示出三个条带,证实分离的TBG没有脱氮化,保留了其结构。凝集素印迹分析和IEF可以被认为是研究TBG糖基化的有用工具。
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