Transthyretin microheterogeneity and thyroxine binding are influenced by non-amino acid components and glutathione constituents

Biochemical and Biophysical Research Communications
T PetterssonH Jörnvall


Two non-amino acid components as well as the glutathione constituents in labile associations with transthyretin (TTR) have been detected by preparative polyacrylamide gel electrophoresis from preparations isolated by affinity chromatography on Sepharose-bound retinol-binding protein (RBP). Incubation of native or reduced TTR with these novel components influenced the quaternary structure and caused reactions with reduced TTR in particular. Reduction of isolated TTR monomers released cysteine from the quantitatively major monomer, but non-amino-acid components from another dominating monomer. The reaction patterns also influence thyroxine (T4) binding. These relationships indicate that interactions in serum of TTR with constituents of glutathione and components different from T4 and retinol-RBP are important for the metabolism and function of TTR.


Feb 1, 1991·Journal of Protein Chemistry·R KaiserH Jörnvall
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Nov 17, 2006·Amyloid : the International Journal of Experimental and Clinical Investigation : the Official Journal of the International Society of Amyloidosis·Yoshiki SekijimaJeffery W Kelly
Jul 1, 1992·Clinical Genetics·I L AlvesM J Saraiva

Related Concepts

Chromatography, Affinity
Molecular Sieve Chromatography
High Pressure Liquid Chromatography Procedure
Cysteine Hydrochloride
Protein Denaturation
Thyroxine-Binding Proteins
Macromolecular Compounds

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