Saito F, Yanagisawa K, Miyatake T
Department of Neurology, School of Medicine, Tokyo Medical and Dental University, Japan.
Brain Res Mol Brain Res. 1993 Jul;19(1-2):171-4. doi: 10.1016/0169-328x(93)90164-k.
The linkage of the glycan chain to the beta/A4 amyloid protein precursor (APP) in cerebrospinal fluid (CSF) was studied by Western blot analysis. The apparent molecular weight of APP in CSF was reduced from 103 to 100 kDa by N-glycanase, and to 96 kDa by O-glycanase treatment, respectively. These data indicate that APP is both N- and O-glycosylated in one molecule. The extent of glycosylation of APP was not altered in the CSF from patients with Alzheimer's disease.
通过蛋白质免疫印迹分析研究了脑脊液（CSF）中聚糖链与β/A4淀粉样蛋白前体（APP）的连接。用N-糖苷酶处理后，脑脊液中APP的表观分子量从103 kDa降至100 kDa，用O-糖苷酶处理后降至96 kDa。这些数据表明APP在一个分子中同时进行了N-糖基化和O-糖基化。阿尔茨海默病患者脑脊液中APP的糖基化程度没有改变。
