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Inhibition of disulfide bonding of von Willebrand protein by monensin results in small, functionally defective multimers
The biosynthesis of von Willebrand protein by human endothelial cells was impaired by the presence of the carboxylic ionophore monensin. Several processing steps that have been localized to the Golgi apparatus were affected in a dose-dependent manner, including carbohydrate processing, dimer multime...
| Formato: | Texto |
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| Lenguaje: | English |
| Publicado: |
The Rockefeller University Press
1985
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113641/ https://www.ncbi.nlm.nih.gov/pubmed/3924917 |