A novel investigation of the interaction of proteins with sodium dodecylbenzyl sulfonate

作者：Gao, HW^*; Shen, R; Zhang, YL

来源：Russian Journal of Physical Chemistry, 2004, 78(7): 1149-1155.

• NUCLEIC-ACIDS
• TRACE AMOUNTS
• DIFFERENCE SPECTROSCOPY
• SELECTIVE DETERMINATION
• LANGMUIR AGGREGATION
• SERUM-ALBUMIN
• COMPLEXES
• DNA
• CHROMOPHORE
• SCATTERING

The microsurface adsorption-spectral correction (MSASC) technique was applied to the interactions of sodium dodecylbenzyl sulfonate (SDBS) with pyronin B (PRB) and three kinds of proteins: bovine serum albumin (BSA), myoglobin (Mb), and ovalbumin (OVA). The aggregations obeyed the Langmuir isothermal adsorption. The characterization of the SDBS-PRB and SDBS-protein aggregates was performed. The break point approach was applied to examine the binding constants obtained by the MSASC technique. Results showed that the products PRB (.) SDBS, SDBS110 (.) BSA, SDBS69 (.) OVA, and SDBS23 (.) Mb are formed at pH 2.81 at 30degreesC. The aggregation of SDBS on proteins is applied to analysis of samples with satisfactory results.

• 出版日期2004-7
• 单位同济大学; 污染控制与资源化研究国家重点实验室