Affinity labeling of human serum prealbumin with N-bromoacetyl-L-thyroxine.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference16 articles.
1. Vitamin A Transport and Retinol-Binding Protein Metabolism
2. Structure of human plasma prealbumin at 2.5 A resolution
3. The Amino Acid Sequence of Human Plasma Prealbumin
4. Negative cooperativity in the binding of thyroxine to human serum prealbumin
5. Affinity labeling of the thyroxine binding domain of human serum prealbumin with dansyl chloride
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1. Rigorous Treatment of Multispecies Multimode Ligand−Receptor Interactions in 3D-QSAR: CoMFA Analysis of Thyroxine Analogs Binding to Transthyretin;Journal of Chemical Information and Modeling;2011-04-08
2. The thyroid hormone transporters MCT8 and MCT10 transport the affinity-label N-bromoacetyl-[125I]T3 but are not modified by it;Molecular and Cellular Endocrinology;2011-04
3. Cell and Molecular Biology of Transthyretin and Thyroid Hormones;International Review of Cytology;2007
4. Change in structure of the N-terminal region of transthyretin produces change in affinity of transthyretin to T4 and T3;FEBS Journal;2006-07-28
5. The Evolution of Transthyretin Synthesis in Vertebrate Liver, in Primitive Eukaryotes and in Bacteria;Clinical Chemistry and Laboratory Medicine;2002-01-10
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