D'Andrea G, D'Alessandro A M, Salucci M L, Oratore A
Department of Sciences and Biomedical Technologies and Biometrics, University of L'Aquila, Italy.
J Protein Chem. 1994 Jan;13(1):31-6. doi: 10.1007/BF01891990.
Human seminal transferrin (HSmT) is an iron-containing glycoprotein whose structural properties have not been adequately investigated. The carbohydrate content of the purified glycoprotein amount to 6.1%, and monosaccharide analysis revealed the major oligosaccharide moiety to be of the N-glycoside type. The carbohydrate chains were released from the iron-free form by digestion with peptide N-glycosidase F (PNGase F) in the presence of detergents such as SDS and beta-octylglucoside. After ethanol precipitation and fractionation on Bio-Gel P-6 and Bio-Gel P-2, the oligosaccharide was further purified on Mono-Q and desalted on Bio-Gel P-2. By 600-MHz 1H-NMR spectroscopy, the primary structure of the major N-linked oligosaccharide component was established to be: [formula: see text]
人精液转铁蛋白(HSmT)是一种含铁糖蛋白,其结构特性尚未得到充分研究。纯化糖蛋白的碳水化合物含量为6.1%,单糖分析表明主要的寡糖部分为N-糖苷类型。在SDS和β-辛基葡糖苷等去污剂存在的情况下,通过用肽N-糖苷酶F(PNGase F)消化,从无铁形式中释放出碳水化合物链。经过乙醇沉淀以及在Bio-Gel P-6和Bio-Gel P-2上分级分离后,寡糖在Mono-Q上进一步纯化,并在Bio-Gel P-2上去盐。通过600兆赫兹的1H-NMR光谱,确定主要N-连接寡糖成分的一级结构为:[化学式:见原文]