4.50—Polarographic investigation of conformational changes of human serum albumin: Part I. Unfolding of human serum albumin by urea
✍ Scribed by Josef Chmelik; Vitěz Kalous
- Publisher
- Elsevier Science
- Year
- 1982
- Weight
- 421 KB
- Volume
- 141
- Category
- Article
- ISSN
- 0022-0728
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
A method for studying conformational changes induced in the human albumin molecule, either in its purified form or in serum, is described. Plates were coated with albumin or human serum at varying pHs and were reacted with peroxidase-labeled anti-albumin monoclonal antibodies of different specificit
The mechanism of binding of molecular probe eosin to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding center on human serum albumin molecule for eosin is determined. The amino acid residues of albumin molecule, participating in binding of eosin a
The effect of guanidine hydrochloride (GnHCl) on the global stability of human serum albumin (HSA) has been studied by fluorescence and circular dichroism spectroscopic measurements. The differential stability of native conformation of three HSA domains were explored by using domain-specific ligands
## Abstract The binding interaction of adenosine with human serum albumin (HSA) was investigated under simulative physiological conditions by fluorescence spectroscopy in combination with a molecular modeling method. A strong fluorescence quenching reaction of adenosine to HSA was observed and the