The effect of urea as an electrophoretic buffer solution modifier on the ion-association (IA) capillary electrophoresis (CE) separation of four anionic metal complexes of Al(III), Co(III), Cr(III), and Fe(III) with 2,2'-dihydroxyazobenezene-5,5'-disulfonate (DHABS) using a hydrophobic ion-association agent, tetrapentylammonium bromide, was studied. The mutual separation of the four anionic metal-DHABS complexes was not achieved without the addition of urea in the electrophoretic buffer solution. However, the addition of 1.5 M urea in the electrophoretic buffer solution brought about a complete separation of the four metal complexes. The ion-association constants between all metal-DHABS complexes and tetrapentylammonium in an aqueous urea solution were smaller than those in a neat aqueous solution. This indicates the hydrophobic interaction contributing to the ion-association between analytes and ion-association agent during IA-CE separation processes can be controlled with the addition of urea to the electrophoretic buffer solution. Another advantage of adding urea was a substantial enhancement of separation efficiency with a reduction of the half-bandwidth of the peaks. Also, a reduction of the electrophoretic mobility of the electroosmotic flow when urea was added was much less than when organic solvents were used.
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http://dx.doi.org/10.2116/analsci.26.1151 | DOI Listing |
J Agric Food Chem
December 2024
Ecofood Institute, College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, China.
Biochim Biophys Acta Proteins Proteom
September 2024
Institute of Protein Research, Russian Academy of Sciences, 4 Institutskaya Street, 142290 Pushchino, Russia. Electronic address:
The discovery of a subunit exchange in some oligomeric proteins, implying short-term dissociation of their oligomeric structure, requires new insights into the role of the quaternary structure in oligomeric protein stability and function. Here we demonstrate the effect of pH, protein concentration, and urea on the efficiency of GroES heptamer (GroES) subunit exchange. A mixture of equimolar amounts of wild-type (WT) GroES and its Ala97Cys mutant modified with iodoacetic acid (97-carboxymethyl cysteine or CMC-GroES) was incubated in various conditions and subjected to isoelectric focusing (IEF) in polyacrylamide gel.
View Article and Find Full Text PDFJ Nanobiotechnology
May 2024
Department of General Surgery, The First Affiliated Hospital of Shandong First Medical University, Shandong Provincial Qianfoshan Hospital, No. 16766, Jingshi Road, Jinan, 250014, China.
Background: Advanced hepatocellular carcinoma (HCC) can be treated with sorafenib, which is the primary choice for targeted therapy. Nevertheless, the effectiveness of sorafenib is greatly restricted due to resistance. Research has shown that exosomes and circular RNAs play a vital role in the cancer's malignant advancement.
View Article and Find Full Text PDFBiochem Cell Biol
June 2024
Centre for Forest Biology, Department of Biology, University of Victoria, Victoria, BC V8W 2Y2, Canada.
Sperm nuclear basic proteins (SNBPs) were isolated from extracted antheridia-rich male gametophytes raised from spores of the swordfern, . Electrophoretic (acetic acid-urea PAGE and SDS-PAGE) and chromatographic (rp-HPLC) characterization of the nuclear proteins exhibited the characteristics of the histone (H-type). In both types of gel electrophoresis, histones H1, H2A, and H2B showed an altered electrophoretic mobility corresponding to that which is routinely observed for the histones in other plants.
View Article and Find Full Text PDFAnal Bioanal Chem
March 2024
Faculty of Chemistry, Aalen University, Aalen, Germany.
Characterization at the subunit level enables detailed mass spectrometric characterization of posttranslational modifications (PTMs) of monoclonal antibodies (mAbs). The implemented reduction often leaves the intramolecular disulfide bridges intact. Here, we present a capillary electrophoretic (CE) method based on a neutral-coated capillary for the separation of immunoglobulin G-degrading enzyme of Streptococcus pyogenes (IdeS) digested and reduced mAb subunits followed by mass spectrometry (MS), MS/MS identification, and trapped ion mobility mass spectrometry (timsTOF).
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