Chromium-protein complexation studies by adsorptive cathodic stripping voltammetry and MALDI-TOF-MS
2012 (English)In: Journal of Applied Electrochemistry, ISSN 0021-891X, E-ISSN 1572-8838, Vol. 42, no 5, 349-358 p.Article in journal (Refereed) Published
A methodology using stripping voltammetry has been elaborated to enable sensitive and reliable protein-chromium complexation measurements. Disturbing effects caused by adsorption of proteins on the mercury electrode were addressed. At low concentrations of proteins (< 60-85 nM), chromium-protein complexation measurements were possible. Chromium(VI) complexation was quantitatively determined using differently sized, charged, and structured proteins: serum albumin (human and bovine), lysozyme, and mucin. Generated results showed a strong relation between complexation and protein size, concentration, and the number of amino acids per protein mass. Complexation increased nonlinearly with increasing protein concentrations. The nature of this complexation was based on weak interactions judged from combined results with MALDI-TOF-MS and adsorptive cathodic stripping voltammetry.
Place, publisher, year, edition, pages
2012. Vol. 42, no 5, 349-358 p.
Chromium, Complexation, Lysozyme, Serum albumin, Mucin, Stripping voltammetry
IdentifiersURN: urn:nbn:se:kth:diva-93903DOI: 10.1007/s10800-012-0404-6ISI: 000302410900009OAI: oai:DiVA.org:kth-93903DiVA: diva2:525060
FunderSwedish Research Council
QC 201205042012-05-042012-05-032012-11-26Bibliographically approved