Structure of fibronectin and its fragments in electron microscopy.
Structure of fibronectin and its fragments in electron microscopy.
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电子显微镜下纤连蛋白及其片段的结构。
DOI：
10.1111/j.1432-1033.1982.tb07058.x
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发表时间：
1982
期刊：
影响因子：
--
通讯作者：
Ruoslahti,E
中科院分区：
文献类型：
--
作者：
Price,TM;Rudee,ML;Pierschbacher,M;Ruoslahti,E
人血浆纤维连接蛋白和一系列的大蛋白水解片段进行了分析，通过电子显微镜使用钨阴影碳和聚苯乙烯薄膜。在碳上，完整的纤连蛋白表现为随机卷曲的链，而在聚苯乙烯上，它表现为细长的结构。纤连蛋白的两个片段，Mr=205000和190000，其缺乏纤连蛋白的NH 2末端结构域并保留胶原蛋白结合、细胞附着和肝素结合功能，以及aMr= 170000片段，其保留胶原蛋白结合和细胞附着功能，被视为具有不同程度的球化的杆，而aMr= 100000片段，其仅结合胶原蛋白，这些结果支持了现有的生化证据，即纤连蛋白分子中功能活性的分离是基于不同的结构域，并提供了生化和功能研究未揭示的额外结构域存在的证据。
Human plasma fibronectin and a series of its large proteolytic fragments were analyzed by electron microscopy using tungsten shadowing on carbon and polystyrene films. On carbon, intact fibronectin appeared as a randomly coiled strand, while on polystyrene it appeared as an elongated structure. Two fragments of fibronectin,Mr=205000 and 190000, which lack the NH2‐terminal domain of fibronectin and retain the collagen‐binding, cell‐attachment and heparin‐binding functions, and aMr= 170000 fragment, which retains the collagen‐binding and cell‐attachment functions, were seen as rods with varying degrees of nodularity while aMr= 100000 fragment, which only binds to collagen, had two clear‐cut domains.These results support the existing biochemical evidence that the segregation of the functional activities in the fibronectin molecule is based on distinct structural domains and provides evidence for the existence of an additional structural domain not revealed by biochemical and functional studies.