Schlüter M, Linder D, Geyer R, Hunsmann G, Schneider J, Stirm S
FEBS Lett. 1984 Apr 24;169(2):194-8. doi: 10.1016/0014-5793(84)80317-8.
The glycoprotein from Friend murine leukemia virus was digested with protease from Staphylococcus aureus V8. A glycopeptide comprising the N-terminal glycosylation site (Asn-12) was isolated from the mixture of fragments and analyzed by amino acid sequencing and methylation-capillary gas chromatography-mass spectrometry before and after treatment with sialidase from Vibrio cholerae. Asn-12 was thus found to be substituted by a family of partially sialylated, fucosylated, and intersected glycoprotein N-glycans of the hybrid type.
来自弗氏鼠白血病病毒的糖蛋白用金黄色葡萄球菌V8蛋白酶进行消化。从片段混合物中分离出包含N端糖基化位点(Asn-12)的糖肽,并在用霍乱弧菌唾液酸酶处理前后通过氨基酸测序和甲基化-毛细管气相色谱-质谱法进行分析。结果发现Asn-12被一类部分唾液酸化、岩藻糖基化且相互交叉的杂合型糖蛋白N-聚糖所取代。