Sharma N D, Evans R W, Patel K J, Gorinsky B, Mallet A I, Aitken A
Division of Biochemistry and Molecular Biology, UMDS, Guy's Hospital, London, UK.
Biochim Biophys Acta. 1994 Jun 12;1206(2):286-8. doi: 10.1016/0167-4838(94)90220-8.
In this study we report the number and location of the glycans on PST. Urea PAGE and SDS-PAGE have been used to follow the enzymatic removal of sialic acids and of glycans from PST and the masses of native and deglycosylated PST have been determined by electrospray mass spectrometry. The results are consistent with the presence of a single biantennary glycan chain. As amino acid sequence analysis demonstrated the absence of a glycosylated asparagine at position 25, the glycosylation site is restricted to Asp-497.
在本研究中,我们报告了PST上聚糖的数量和位置。已使用尿素聚丙烯酰胺凝胶电泳(Urea PAGE)和十二烷基硫酸钠聚丙烯酰胺凝胶电泳(SDS-PAGE)来跟踪从PST上酶促去除唾液酸和聚糖的过程,并通过电喷雾质谱法测定了天然和去糖基化PST的质量。结果与单个双天线聚糖链的存在一致。由于氨基酸序列分析表明在第25位不存在糖基化的天冬酰胺,因此糖基化位点限于Asp-497。