Removal of Dodecyl Sulfate Ions Bound to Human and Bovine Serum Albumins Using Sodium Cholate

Abstract

Introduction Sodium dodecyl sulfate SDS is currently a widely used tool in the purification and characterization of proteins in many fields of biochemistry 1. A typical example is SDSpolyacrylamide gel electrophoresis SDS-PAGE , which is conventionally used to determine the molecular weights of proteins 2, 3. In this method, electrophoresis of SDS-protein complexes is carried out under the condition that the dodecyl sulfate DS ions are fully bound to all of the proteins in order to counteract their individual surface charges. Apart from SDS being used solely as a tool, the interaction itself between SDS and proteins has been widely investigated for more than 70 years 4 10. These studies have clarified that SDS induces distinct conformational changes in proteins. In SDS solution, for example, helical structures are partially disrupted in proteins having high helicity, whereas they are partially formed in proteins having low helicity. These structural changes are induced by the binding of DS ions. Therefore, much is known about

Circular Dichroism Spectra of α-Chymotrypsin–SDS Solutions Depend on the Procedure of Their Preparation

“…This indicates that the structure of CHA (with a concentration of 20 or 40 μM, respectively) in the solution containing 6 mM SDS is different than the structure of the protein (with a concentration of 10 or 20 μM, correspondingly) in the solution containing 3 mM SDS. In addition, because the structure is stable, 2-fold dilution of the first solution, 20 (40) μM chymotrypsin with 6 mM SDS, does not lead to the structure adopted by the protein when the corresponding concentration of the protein is mixed in a 1:1 volume ratio with 6 mM SDS.…”

“…As we have shown using the example of CHA and SDS, such an approach is able to provide new insights into protein–surfactant interactions and the mechanism of surfactant-triggered structural transitions in proteins. We hope that our work will encourage others to perform similar studies on different systems using the vast arsenal of experimental methods that are available for investigations of surfactant–protein interactions. ,,− An interesting case study would be ferrocytochrome c for which SDS-induced conformational transitions appear to be reversible …”

Ecological Environment and Pollution Control under the Influence of Modern Biotechnology Development

“…Finally, regional division. In order to effectively control the transfer of pollutants, even in the same treatment area, it is necessary to do a good job in the investigation of hydrology, soil and microbial populations in different intervals, to divide the area, and to take corresponding and differentiated treatment measures [11][12].…”