Abstract

The microphase adsorption-spectral correction (MPASC) technique is described and applied to the study of the interactions of Evans blue (EB) with cetyltrimethylammonium bromide (CTAB) and with four proteins: bovine serum albumin (BSA), myoglobin (Mb), hemoglobin (Hb) and ovalbumin (OVA). EB can be adsorbed on a cationic surfactant and on protein by electrostatic force and the aggregation obeys the Langmuir isotherm. Results have shown that the products are formed as follows: monomer aggregate EB·CTAB, micellar aggregate (EB·CTAB) 78 and protein aggregates (EB 68·BSA), (EB 14·OVA), (EB 126·Mb) and (EB 58·Hb). The adsorption constant of the aggregates are calculated to be K EB·CTAB=2.95×10 6, K EB68·BSA=3.40×10 4, K EB14·OVA=5.20×10 2, K EB126·Mb=6.81×10 2 and K EB58·Hb=5.73×10 2, respectively. The aggregation of EB in proteins is sensitive in the presence of CTAB and selective in the presence of EDTA and it has been applied to the analysis of samples with satisfactory results.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.