Leushner J R
Biochem Cell Biol. 1987 May;65(5):501-6. doi: 10.1139/o87-064.
A major heteropolysaccharide fraction was isolated from the 7S domain of human placental type IV collagen. Analyses revealed that it was an asparagine-linked oligosaccharide. Characterization using molecular sieve chromatography, exoglycosidase and endoglycosidase digestion, and chemical analysis suggested a bianternnary complex with the following structure: (Formula: see text) A microheterogeneity was noted with respect to the addition of the fucose and sialic acid residues. Analysis of component polypeptides of the 7S fraction following endoglycosidase treatment suggested that the most obvious site of heteropolysaccharide attachment was in a polypeptide of relative mass 40,000. Amino acid analysis of this isolated polypeptide indicated that it was rich in collagenous sequences and also contained half-cystine residues.
从人胎盘IV型胶原的7S结构域中分离出一种主要的杂多糖组分。分析表明它是一种天冬酰胺连接的寡糖。使用分子筛色谱、外切糖苷酶和内切糖苷酶消化以及化学分析进行表征，提示其具有以下结构的双三元复合物：（分子式：见正文）观察到岩藻糖和唾液酸残基添加方面的微不均一性。内切糖苷酶处理后对7S组分的组成多肽进行分析表明，杂多糖附着最明显的位点位于相对分子质量为40,000的一种多肽中。对这种分离出的多肽进行氨基酸分析表明，它富含胶原序列并且还含有半胱氨酸残基。
