Book

Description

The relevance of studies on protein-surfactant interaction comes from the manifold applications of protein-surfactant systems, e.g., from the food industry, pharmaceutical industry and analytical biochemistry. Proteins saturated with SDS are observed to have electrophoretic mobilities through polyacrylamide gels that are inversely proportional to the logarithm of the molecular mass of the protein. The molecular mass is determined by comparison of the mobility of the unknown protein with that of a set of standard marker proteins. Apparently, SDS bound to proteins imposes comparable shapes and net-charge densities on the protein-SDS complexes. The effect of different surfactant head-groups on the complex formation was studied by DLS and fluorescence. The results shown by the denaturation studies of b-cyt-c and h-cyt-c by STS (sodium tetradecyl sulphate) are similar as we have obtained in case of SDS.