Binding studies with recombinant human serum albumin obtained by expression of a synthetic gene in yeast. Stereoselective binding and allosteric interaction with benzodiazepine and coumarin ligands.
The specific ligand binding ability of recombinant human serum albumin produced in yeast using the synthetic gene was studied by affinity chromatographic method. It was found that synthetic protein possesses those stereoselective binding and binding interactions for several chiral benzodiazepine and coumarin compounds which are characteristic of the natural human serum albumin, suggesting identical tertiary structures.
Fitos
I
I
Central Research Institute for Chemistry of the Hungarian Academy of Sciences, Budapest.
Visy
J
J
Simoncsits
A
A
D001569:Benzodiazepines / Q000378:metabolism*; D001665:Binding Sites; D002250:Carbon Radioisotopes; D002846:Chromatography, Affinity; D003374:Coumarins / Q000378:metabolism*; D004347:Drug Interactions; D005800:Genes, Fungal; D006801:Humans; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D012709:Serum Albumin / Q000235:genetics / Q000378:metabolism*; D013237:Stereoisomerism
D002250:Carbon Radioisotopes; D003374:Coumarins; D011994:Recombinant Proteins; D012709:Serum Albumin; D001569:Benzodiazepines; C030123:coumarin