PubMed Health⌕ Search

Biomedical subjects

A K Bordbar

Publications and source records attributed to A K Bordbar.

2 recordsLinked to original sources

Analysis of ligand binding process using binding capacity concept.

Binding capacity is the homotropic second derivative of the binding potential with respect to the chemical potential of the ligand. It provides a measure of steepness of the binding isotherm and represents the extent of cooperativity. In the present study, the shape of the binding capacity curve for various systems was investigated and the relation between binding capacity and the extent of cooperativity examined. In this regard, a novel linear graphical method was introduced for binding data analysis. The stoichiometry of binding and the extent of cooperativity can be determined by this method. This method has been successfully applied to various systems such as binding of oxygen to hemoglobin, warfarin to human serum albumin and dodecyltrimethylammonium bromide to alpha-amylase.

Hemoglobins↗

Mechanism of denaturation of bovine serum albumin by dodecyl trimethylammonium bromide.

Bovine serum albumin (BSA) denaturation has been extensively studied by different anionic and cationic surfactant. Dodecyl trimethylammonium bromide (DTAB) is a cationic surfactant, and it is suggested that it binds to the C-terminal section of BSA. In the present study, the thermodynamical denaturation of BSA by dodecyl trimethylammonium bromide (DTAB) has been studied with various experimental techniques. Equilibrium dialysis, thermal denaturation, gel electrophoresis, titration microcalorimetry at pH 7, I = 0.005, and different temperatures were all performed. The enthalpy obtained from the van't Hoff relation and calorimetry method as well as electrophoresis results were utilized to explain the BSA tranistion state. Major findings included: the binding isotherm shifts at a low free concentrations of DTAB and at a higher temperature suggest endothermicity for enthalpy of interaction; the calorimetry enthalpy (delta Hcal) of interaction was smaller than the van't Hoff enthalpy (delta HvH) for BSA-DTAB interaction; and the aggregation of BSA increased with increasing DTAB concentration. This study suggests that BSA unfolding induced by DTAB follows a multistate transition model and does not follow the two-state mechanism assumed for most single subunit proteins.

Animals↗