essay代写-n链糖基化和o链糖基化。本文讨论了两种类型的糖化反应。它是n链糖基化和o链糖基化。从整体机制分析,可以了解e -选择素配体在这一过程中的作用。n链糖基化是一个高度保守的、独特的过程。o型糖基化是一种糖分子,与蛋白质内氨基酸残基中的氧原子相连。许多实证研究表明,e -选择素配体在糖基化过程中起决定性作用。其中,本分析中讨论的特异性E-slectin配体是CD44和CD24[37]。由于其独特的功能,人们发现它们是有效的癌症生物标记。这有助于了解与癌有关的确切机制。接下来论文范文essay代写-n链糖基化和o链糖基化分享给留学生阅读。

Two kinds of glycsylation have been discussed in this analysis. It is the N-linked glycosylation and the O-linked glycosylation. From analysis of the overall mechanism, there can be understanding of the function of the E-selectin ligand in this process. The process of N-Linked glycosylation is highly conserved and an unique process. O-linked glycosylation is a sugar molecule that is attached to an oxygen atom in the amino acid residue within the protein. A number of empirical researches have been undertaken to showcase that there is a definitive role of the E-selectin ligand in the process of glycosylation. Of this, the specific E-slectin ligand that has been discussed in this analsysis is the CD44 and the CD24 [37]. Owing to their distinctive functionality, it has been found that they serve as effective cancer biomarkers. This serves in understanding about the exact mechanisms that are involved carcinoma.
Initially, Cd44 is focused. CD44 function is affect by glycosylation type. It has been found that each kind of the glycosylation has an impact on the CD44 mediated cell binding in hyaluronan (HA). Exact heuristics of the process is yet to be found. From empirical research, it has been found that four factors determine how the CD44 binds to the HA. They are the terminal α2, 3-linked sialic acid on N-linked oligosaccharides that inhibit the biding. The first N-linked N-acetylglucosamine residues, if found to increase the binding of the (O)-linked glycans on N-deglycosylated. CD44 enhanced binding and finally N-acetylgalatosamine was also found to be incorporated in to the non-N-linked glycans. Empirical research has proven that E-selectin ligand activity of CD44 is determined by expression of N-linked glycosylation in breast cancer cells[8].

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