Post-translational assembly and glycosylation of laminin subunits in parietal endoderm-like F9 cells

壁层内胚层样F9细胞中层粘连蛋白亚基的翻译后组装和糖基化

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Abstract

Non-reducing and reducing sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of laminin synthesized in parietal endoderm-like F9 cells demonstrated that only AB1B2 complex goes through intracellular traffic for oligosaccharide side-chain processing and secretion. Glycosylation was not necessary for subunit assembly. Assembly was suggested to proceed through B1B2 to AB1B2. Among the pools of monomer subunits, the B2 pool was smallest.

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