DIMERIC CHARACTER OF FIBRONECTIN, A MAJOR CELL SURFACE-ASSOCIATED GLYCOPROTEIN
DIMERIC CHARACTER OF FIBRONECTIN, A MAJOR CELL SURFACE-ASSOCIATED GLYCOPROTEIN
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DOI：
10.1016/0006-291x(77)90359-x
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发表时间：
1977-01-01
影响因子：
3.1
通讯作者：
VAHERI, A
中科院分区：
文献类型：
--
作者：
KESKIOJA, J;MOSHER, DF;VAHERI, A
暴露的蛋白质培养的鸡和人的成纤维细胞标记乳过氧化物酶催化碘化和分析聚丙烯酰胺凝胶电泳在十二烷基硫酸钠。两种细胞类型的提取物都含有纤连蛋白的特征性的、重标记的条带（MW = 2.2 × 106）。105)在用2-巯基乙醇还原后进行分析。在没有预先减少的情况下，2.2 ×105 MW条带缺失，被4.4 × 105的标记条带代替。105和非常高的分子量。成纤维细胞表面纤连蛋白，如从血浆中纯化的纤连蛋白，显然是由2个高分子量多肽通过二硫键保持在一起;二聚体可以另外形成二硫键键合的多聚体。
Exposed proteins of cultured chick and human fibroblasts were labeled by lactoperoxidase-catalyzed iodination and analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate. Extracts from both cell types contained the characteristic, heavily labeled band of fibronectin (MW = 2.2 .times. 105) were analyzed after reduction with 2-mercaptoethanol. Without prior reduction the 2.2 .times. 105 MW band was missing and replaced by labeled bands of 4.4 .times. 105 and of very high molecular weight. Fibroblast cell-surface fibronectin, like the fibronectin purified from plasma, is apparently composed of 2 high molecular weight polypeptides held together by disulfide bonds; the dimer may in addition form disulfide-bonded multimers.