Investigation on molecular non-covalent interaction in the sodium dodecyl benzene sulfonate-polychrome blue B-protein replacement reaction
✍ Scribed by Hong-Wen Gao; Ji-Rong Wu; Rong Shen
- Publisher
- John Wiley and Sons
- Year
- 2010
- Tongue
- English
- Weight
- 563 KB
- Volume
- 22
- Category
- Article
- ISSN
- 0256-7660
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✦ Synopsis
Abstract
The molecular noncovalent interaction often originates from the electrostatic attraction and accords with the Langmuir isothermal adsorption. The sodium dodecyl benzene sulfonate (SDBS)‐polychrome blue B (PCB>protein bovine serum albumin (BSA), ovalbumin (OVA) and myoglobin (MB)] ternary reaction has been investigated at pH 3.88. Protein to replace PCB from the PCB‐SDBS binding product was used to characterize the assembly of an invisible‐spectral compound, SDBS, on proteins by measuring the variation of FCB light‐absorption by tbe micro‐surface adsorption‐spectral correction (MSASC) technique. The effect of ionic strength and temperature on the aggregation was studied. Results showed that the aggregates SDBS~92~·BSA, SDBS~58~·VA and SDBS~15~·MB at 30 C and SDBS~83~·BSA. SDBS~39~·OVA and SDBS~10~·MB at 50 °C are formed.