摘要
The molecular non-covalent 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 PCB light-absorption by the microsurface adsorption-spectral correction (MSASQ technique. The effect of ionic strength and temperature on the aggregation was studied. Results showed that the aggregates SDBS(92)(.)BSA, SDBS(58)(.)OVA and (SDBS15MB)-M-. at 30 degreesC and SDBS(83)(.)BSA, SDBS(39)(.)OVA and (SDBS10MB)-M-. at 50 degreesC are formed.
The molecular non-covalent 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 PCB light-absorption by the microsurface adsorption-spectral correction (MSASQ technique. The effect of ionic strength and temperature on the aggregation was studied. Results showed that the aggregates SDBS(92)(.)BSA, SDBS(58)(.)OVA and (SDBS15MB)-M-. at 30 degreesC and SDBS(83)(.)BSA, SDBS(39)(.)OVA and (SDBS10MB)-M-. at 50 degreesC are formed.
