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Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin
BACKGROUND: Iophenoxic acid is an iodinated radiocontrast agent that was withdrawn from clinical use because of its exceptionally long half-life in the body, which was due in part to its high-affinity binding to human serum albumin (HSA). It was replaced by Iopanoic acid, which has an amino rather t...
Autores principales: | , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2011
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3104944/ https://www.ncbi.nlm.nih.gov/pubmed/21501503 http://dx.doi.org/10.1186/1472-6807-11-18 |