Expression of a human serum albumin variant with high affinity for thyroxine.

Abstract

In this study a protein expression system was used to synthesize recombinant human serum albumin containing a mutation that has been shown to result in familial dysalbuminemic hyperthyroxinemia. Equilibrium dialysis was used to measure the binding of this recombinant human serum albumin with thyroxine. The association constant determined for the binding of this human serum albumin variant with thyroxine was shown to be 65-fold greater than that of recombinant normal human serum albumin.

• Authors: C E Petersen, C E Ha, M Mandel, N V Bhagavan
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 214 Issue 3 Pg. 1121-9 (Sep 25 1995) ISSN: 0006-291X [Print] United States
• PMID: 7575519 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Recombinant Proteins
• Serum Albumin
• Trypsin
• Thyroxine

Topics

• Amino Acid Sequence
• Binding Sites
• Cloning, Molecular
• Gene Expression
• Genetic Diseases, Inborn (genetics, metabolism)
• Genetic Variation
• Humans
• Kinetics
• Liver (metabolism)
• Molecular Sequence Data
• Mutation
• Pichia
• Polymerase Chain Reaction
• Recombinant Proteins (biosynthesis, metabolism)
• Reference Values
• Serum Albumin (biosynthesis, genetics, metabolism)
• Thyroxine (metabolism)
• Trypsin