人类α干扰素2是O-glycosylated自然。
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阿道夫GR, Kalsner我Ahorn H,做Maurer-Fogy我,才能证明K
人类α干扰素2是O-glycosylated自然。
j . 1991 276年6月1;(Pt 2): 511 - 8。
- PubMed ID
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2049076 (在PubMed]
- 文摘
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自然人类干扰素α2 (IFN-alpha 2)隔绝人类白细胞干扰素部分纯化的单克隆抗体的制备immunoaffinity色谱法。纯化蛋白的特定活动1.5 x 10(8)国际单位/毫克;据估计占10 - 20%的总白细胞干扰素的抗病毒活性。n端氨基酸序列分析确定了亚种IFN-alpha 2 b和/或IFN-alpha 2 c,而IFN-alpha 2没有检测到。自然IFN-alpha 2被发现的结构不同于它的重组(大肠coli-derived)等价的。首先,反相h.p.l.c.表明自然IFN-alpha 2更亲水然后预期。其次,天然蛋白质的表观分子量由SDS /页面高于重组IFN-alpha 2;轻微的碱性条件下孵化已知消除O-linked碳水化合物导致减少明显的分子质量的重组蛋白。蛋白水解多肽的序列分析,用力推- 106被发现被修改。这些结果表明刺2 - 106自然IFN-alpha O-linked碳水化合物。 Reverse-phase h.p.l.c. as well as SDS/PAGE of natural IFN-alpha 2 showed that glycosylation is heterogeneous. For characterization of the carbohydrate moieties, the protein was treated with neuraminidase and/or O-glycanase and analysed by gel electrophoresis; in addition, glycopeptides obtained by proteinase digestion and separated by h.p.l.c. were characterized by sequence analysis and m.s. Further information on the composition of the glycans was obtained by monosaccharide analysis. The results indicate that natural IFN-alpha 2 contains the disaccharide galactosyl-N-acetylgalactosamine (Gal-GalNAc) linked to Thr-106. In part of the molecules, this core carbohydrate carries (alpha-)N-acetylneuraminic acid, whereas a disaccharide, probably N-acetyl-lactosamine, is bound to Gal-GalNAc in another proportion of the protein. Further glycosylation isomers are present in small amounts. As IFN-alpha 2 is the only IFN-alpha species with a threonine residue at position 106, it may represent the only O-glycosylated human IFN-alpha protein.