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。 本研究的目的是确定果蝇唾液酸基转移酶的糖基化位点的结构和位置 蛋白质，DSiaT。DSiaT代表了动物原生生物谱系中第一个特征化的唾液酸基转移酶(Koles等人)。 2004，JBC 279：4346-435)。这种唾液酸基转移酶与脊椎动物唾液酸转移酶的ST6GAL家族密切相关， 这表明DSiaT可能代表了最进化的古代类型的Matazoan唾液酸基转移酶。

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. The goal of this study was to determine the structure and position of glycosylation sites on the Drosophila sialyltransferase protein, DSiaT. DSiaT represents the first characterized sialyltransferase in the protostome lineage of animals (Koles et al. 2004, JBC 279: 4346-435). This sialyltransferase is closely related to the ST6GAL family of vertebrate sialyltransferases, which indicates that DSiaT may represent the most evolutionary ancient type of matazoan sialyltransferases.