Structural analysis of three subunits of laminin from teratocarcinoma-derived parietal endoderm cells.
Structural analysis of three subunits of laminin from teratocarcinoma-derived parietal endoderm cells.
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来自畸胎癌来源的壁层内胚层细胞的层粘连蛋白的三个亚基的结构分析。
DOI：
10.1016/0012-1606(83)90367-6
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发表时间：
1983
影响因子：
2.7
通讯作者：
Dietzschold,B
中科院分区：
文献类型：
--
作者：
Howe,CC;Dietzschold,B
层粘连蛋白亚基的三条多肽链的结构和每条多肽链中糖基化位点的数量通过高效液相色谱法使用肽图谱来确定。对从衣霉素（TM）处理的细胞中分离的[35 S]甲硫氨酸标记的糖基化不足的层粘连蛋白的分析表明，层粘连蛋白的三个亚基含有独特的多肽链。[3 H]葡糖胺标记的糖基化层粘连蛋白亚基的分析表明，它们是唾液酸化的，每个亚基有11-14个糖基化位点。
The structure of the three polypeptide chains of the laminin subunits and the number of glycosylation sites in each polypeptide chain were determined using peptide mapping by high-performance liquid chromatography. Analysis of the [35S]methionine-labeled underglycosylated laminin isolated from tunicamycin (TM)-treated cells revealed that the three subunits of laminin contain unique polypeptide chains. Analysis of [3H]glucosamine-labeled glycosylated laminin subunits showed that they are sialylated and that each subunit has 11–14 glycosylation sites.