蛋白质糖基化的鉴定和定量

Ziv Roth, G. Yehezkel, I. Khalaila
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引用次数: 120

摘要

糖基化是蛋白质翻译后最丰富的修饰之一,越来越多的证据表明,真核生物中绝大多数蛋白质都是糖基化的。糖基化在蛋白质折叠、相互作用、稳定性和移动性以及信号转导中发挥作用。因此,通过调节蛋白质活性,糖基化参与细胞的正常功能和疾病的发生。事实上,在过去的几十年里,人们越来越认识到蛋白质糖基化的重要性,因为异常的糖基化与代谢、神经退行性和肿瘤疾病有关。因此,在生物化学和糖生物学的基础科学以及应用科学,特别是生物医学和生物技术中,蛋白基低聚糖的鉴定和定量变得越来越重要。在这里,我们回顾了鉴定和定量低聚糖,特别是N和o糖基化蛋白的最先进的方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Identification and Quantification of Protein Glycosylation
Glycosylation is one of the most abundant posttranslation modifications of proteins, and accumulating evidence indicate that the vast majority of proteins in eukaryotes are glycosylated. Glycosylation plays a role in protein folding, interaction, stability, and mobility, as well as in signal transduction. Thus, by regulating protein activity, glycosylation is involved in the normal functioning of the cell and in the development of diseases. Indeed, in the past few decades there has been a growing realization of the importance of protein glycosylation, as aberrant glycosylation has been implicated in metabolic, neurodegenerative, and neoplastic diseases. Thus, the identification and quantification of protein-borne oligosaccharides have become increasingly important both in the basic sciences of biochemistry and glycobiology and in the applicative sciences, particularly biomedicine and biotechnology. Here, we review the state-of-the-art methodologies for the identification and quantification of oligosaccharides, specifically N- and O-glycosylated proteins.
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