GLYCAN STRUCTURE & POSITION OF GLYCOSYLATION SITES ON DSIAT

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 果蝇唾液酸转移酶(DsiaT)基因与脊椎动物ST6Gal唾液酸转移酶家族关系密切，近年来已被鉴定，并决定了其体外酶活性和受体特异性。作为体外受体，这种酶被发现偏爱糖蛋白N-连接的糖链上的末端LacdiNAc和LacNAc残基(Koles等人，2004年)。在这项合作工作中，我们对DSiaT上的多糖结构和糖基化位点(S)进行了分析。我们的数据表明，DSiaT的N-糖链结构以岩藻糖化的高甘露糖型(Man3GlcNAc2Fuc1)为主要成分。我们目前正在绘制N-糖基化位点的图谱。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Drosophila sialytransferase (DSiaT) gene, which is closely related to the vertebrate ST6Gal sialytransferase family has been characterized recently and has determined the in vitro enzymatic activity and acceptor specificity. As in vitro acceptors, this enzyme was found to prefer terminal LacdiNAc and LacNAc residues found on N-linked glycans of glycoproteins (Koles, et al., 2004). In this collaboration work, we are performing the analysis of glycan structure and the site(s) of glycosylations on the DSiaT. Our data show that the N-glycan structure of the DSiaT has a fucosylated high-mannose type (Man3GlcNAc2Fuc1) as the main component. We are currently working on the mapping of N-glycosylation sites.