Protein binding methodology: comparison of equilibrium dialysis and frontal analysis chromatography in the study of salicylate binding
Autor: | Y.T. Oester, S. Keresztes-Nagy, J.F. Zaroslinski, Roland F. Mais |
---|---|
Rok vydání: | 1972 |
Předmět: |
Reproducibility
Carbon Isotopes Chromatography Binding Sites Chemistry Osmolar Concentration Biophysics Cell Biology Plasma protein binding Human serum albumin Biochemistry Salicylates Gel permeation chromatography Evaluation Studies as Topic medicine Chromatography Gel Humans Equilibrium dialysis Binding site Molecular Biology Dialysis Serum Albumin medicine.drug Protein Binding |
Zdroj: | Analytical biochemistry. 48(1) |
ISSN: | 0003-2697 |
Popis: | The binding of salicylate to human serum albumin (HSA) has been investigated and compared by equilibrium dialysis (ED) and frontal gel chromatography (GELFAC). The data obtained do not fit the single-site binding equation, but could be resolved by a computer program into 2 sets of binding sites with n1 = 1.28, n2 = 3.80, K1 = 70,700 M−1, and K2 = 3300 M−1. The reproducibility of the data provided by GELFAC was far superior to that obtained with ED in spite of the fact that in both cases radioassay was employed. Consequently, analytical errors and bag binding did not appear to be contributory factors to the poor reproducibility of the ED data. |
Databáze: | OpenAIRE |
Externí odkaz: |