Salinovich O, Montelaro R C
Anal Biochem. 1986 Aug 15;157(1):19-27. doi: 10.1016/0003-2697(86)90190-9.
We describe here a two-dimensional mapping procedure which is capable of resolving glycopeptides isolated by lectin affinity chromatography from radioiodinated tryptic digests of glycoproteins. Glycopeptide maps were successfully produced for the model proteins alpha 1-acid glycoprotein and fetuin, as well as for the two surface glycoproteins gp90 and gp45 from equine infectious anemia virus (EIAV). Differences were detected in the glycopeptide maps obtained for the gp90 and gp45 components from two antigenically distinct strains of EIAV, demonstrating the ability of this procedure to detect variations in glycosylation in closely related glycoproteins. Thus this glycopeptide mapping technique provides a simple, rapid method to study changes in glycopeptides requiring only micrograms of glycoprotein.
我们在此描述一种二维映射程序，该程序能够解析通过凝集素亲和色谱法从糖蛋白的放射性碘化胰蛋白酶消化物中分离出的糖肽。已成功生成了模型蛋白α1-酸性糖蛋白和胎球蛋白以及马传染性贫血病毒（EIAV）的两种表面糖蛋白gp90和gp45的糖肽图谱。在从两种抗原性不同的EIAV毒株获得的gp90和gp45组分的糖肽图谱中检测到差异，证明了该程序检测密切相关糖蛋白中糖基化变化的能力。因此，这种糖肽映射技术提供了一种简单、快速的方法来研究仅需微克级糖蛋白的糖肽变化。
