Lipniunas P, Grönberg G, Krotkiewski H, Angel A S, Nilsson B
Department of Carbohydrate Chemistry, University of Lund, Sweden.
Arch Biochem Biophys. 1993 Jan;300(1):335-45. doi: 10.1006/abbi.1993.1046.
A mouse immunoglobulin A monoclonal antibody was isolated from hybridoma culture fluid by affinity chromatography. Chemical analysis of the intact antibody showed a monosaccharide composition, which besides mannose also contained monosaccharides commonly found in N-linked complex type of carbohydrate structures. No N-acetylgalactosamine was found showing the absence of O-linked oligosaccharides. The carbohydrate chains were released from the polypeptide and after fractionation on immobilized concanavalin A and high-performance ion-exchange chromatography structural analysis was performed. The structures were determined by chemical analyses, periodate oxidation in combination with fast atom bombardment mass spectrometry, and 500 MHz 1H NMR spectroscopy. The data revealed a great structural heterogeneity, including partially sialylated bi- and triantennary type of structures. Both types contained in addition species with branches terminated by Gal alpha 1-3Gal sequences.
通过亲和层析从杂交瘤培养液中分离出一种小鼠免疫球蛋白A单克隆抗体。对完整抗体的化学分析显示其单糖组成，除了甘露糖外，还含有N-连接复合型碳水化合物结构中常见的单糖。未发现N-乙酰半乳糖胺，表明不存在O-连接寡糖。碳水化合物链从多肽上释放出来，经固定化伴刀豆球蛋白A分级分离和高效离子交换色谱后进行结构分析。通过化学分析、高碘酸盐氧化结合快原子轰击质谱以及500 MHz 1H NMR光谱确定结构。数据显示出很大的结构异质性，包括部分唾液酸化的双天线和三天线类型结构。两种类型还都包含具有由Galα1-3Gal序列终止分支的种类。
