Expression of a human serum albumin fragment (consisting of subdomains IA, IB, and IIA) and a study of its properties. IUBMB Life 1999 Aug;48(2):169-74
Date
05/04/2000Pubmed ID
10794593DOI
10.1080/713803501Scopus ID
2-s2.0-0032753793 (requires institutional sign-in at Scopus site) 15 CitationsAbstract
Site-directed mutagenesis and a yeast expression system were used to synthesize a human serum albumin (HSA) fragment (amino acids 1-297). The HSA fragment (half HSA) was evaluated with a number of biophysical techniques and found to be similar to the corresponding region in wild-type HSA. Specifically, the circular dichroism spectra of half HSA and wild-type HSA were superimposable, indicating that the highly alpha-helical secondary structure of wild-type HSA is preserved in half HSA. Additionally, half HSA was partially reactive with a polyclonal antibody against authentic HSA. Half HSA, which contains subdomain IIA, had an affinity for thyroxine and several thyroxine analogs, similar to that observed previously for wild-type HSA. This study suggests that the production of recombinant HSA fragments will be useful for the study of HSA ligand interactions.
Author List
Park DS, Petersen CE, Ha C, Harohalli K, Feix JB, Bhagavan NVAuthor
Jimmy B. Feix PhD Professor in the Biophysics department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Biophysical PhenomenaBiophysics
Circular Dichroism
Electron Spin Resonance Spectroscopy
Gene Expression
Humans
Kinetics
Ligands
Mutagenesis, Site-Directed
Peptide Fragments
Pichia
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins
Serum Albumin
Thyroxine
