Hayes G R, Enns C A, Lucas J J
Department of Biochemistry and Molecular Biology, SUNY Health Science Center, Syracuse 13210.
Glycobiology. 1992 Aug;2(4):355-9. doi: 10.1093/glycob/2.4.355.
The human transferrin receptor is a glycoprotein containing three N-linked and one O-linked glycosylation sites. Tryptic digestion of the receptor, followed by chromatography on BioGel P-2 and reverse-phase HPLC, yields a glycopeptide (amino acids 101-120) containing the O-linked site. Amino acid sequence analysis reveals that the site of O-glycosylation is Thr-104. Mass spectral analysis is consistent with the presence of a Gal-GalNAc core with predominantly two sialic acid residues.
人转铁蛋白受体是一种糖蛋白,含有三个N - 连接和一个O - 连接糖基化位点。用胰蛋白酶消化该受体,随后在BioGel P - 2上进行色谱分离并进行反相高效液相色谱分析,得到一个包含O - 连接位点的糖肽(氨基酸101 - 120)。氨基酸序列分析表明,O - 糖基化位点是苏氨酸 - 104。质谱分析结果与主要带有两个唾液酸残基的Gal - GalNAc核心结构的存在相一致。