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Title: Study of the interaction of proteins with curcumin and SDS and its analytical application. Author: Wang F, Yang J, Wu X, Liu S. Journal: Spectrochim Acta A Mol Biomol Spectrosc; 2005 Sep; 61(11-12):2650-6. PubMed ID: 16043060. Abstract: It is found that protein and sodium dodecyl sulphonate (SDS) can enhance resonance light scattering (RLS) of curcumin (CU). Based on this phenomenon, a new quantitative method for protein in aqueous solution has been developed. In the BR (pH 3.5) buffer, the RLS intensity of CU-SDS system is greatly enhanced by protein. The enhanced RLS is proportional to the concentration of protein in the range of 0.00020-20.0 microgml(-1) for bovine serum albumin (BSA) and 0.00040-1.0 microgml(-1) for human serum albumin (HSA) and their detection limits are 0.16 and 0.041 ngml(-1), respectively. An actual sample is satisfactorily determined. In addition, the interaction mechanism between protein and CU-SDS is also studied by using multi-techniques such as RLS, absorption spectroscopy and fluorescence, zeta potential assay measurement.[Abstract] [Full Text] [Related] [New Search]