小鼠免疫球蛋白M中Asn 563的不完全糖基化。
Incomplete glycosylation of Asn 563 in mouse immunoglobulin M.
作者信息
Anderson D R, Samaraweera P, Grimes W J
出版信息
Biochem Biophys Res Commun. 1983 Oct 31;116(2):771-6. doi: 10.1016/0006-291x(83)90591-0.
PMID:6651835
Abstract
Mouse immunoglobulin IgM was prepared from MOPC 104E ascites fluid and [3H]-mannose labeled tumor cells. The purified protein was used to prepare Fc fragments which were cleaved by cyanogen bromide. Gel filtration allows complete separation of the C-terminal glycosylation site. Amino acid and carbohydrate analyses show that Asn 563 of murine IgM is glycosylated only about 44% of the time.
摘要
小鼠免疫球蛋白IgM是从MOPC 104E腹水和[3H]-甘露糖标记的肿瘤细胞中制备的。纯化后的蛋白质用于制备经溴化氰裂解的Fc片段。凝胶过滤可完全分离C端糖基化位点。氨基酸和碳水化合物分析表明，小鼠IgM的天冬酰胺563仅约44%的时间被糖基化。
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