Chemical modification of human albumin at cys34 by ethacrynic acid: structural characterisation and binding properties

摘要: Derivatization of the free cys34 in human albumin, which is reported to occur under physiological conditions, has been performed vitro by reaction protein with ethacrynic acid. This modification investigated mass spectrometry and circular dichroism. Ethacrynic acid proven bind albumin either covalently non-covalently. post-translational does not determine significant changes secondary structure protein, as shown comparable dichroism spectra native modified proteins. Furthermore, binding properties samples have equilibrium dialysis. The affinity higher sites change for drugs site I, like phenylbutazone, or II, diazepam, while a small but increase observed bilirubin, known III. Nevertheless decreases at lower were both I II.