Binding affinity of aluminium to human serum transferrin and effects of carbohydrate chain modification as studied by HPLC/high-resolution ICP-MS

Speciation of Al in human serum by convective-interaction media fast-monolithic chromatography with inductively coupled plasma mass spectrometric detection

“…However, the main problem in Al speciation remained contamination originating from the chromatographic columns and eluents [23]. The progress in speciation of HMM-Al compounds has been achieved by the use of anion-exchange FPLC columns [25][26][27][28][29]. Different cleaning procedures of the eluents resulted in substantial lowering of the risk of contamination with extraneous Al [18][19][20][25][26][27][28][29].…”

“…The progress in speciation of HMM-Al compounds has been achieved by the use of anion-exchange FPLC columns [25][26][27][28][29]. Different cleaning procedures of the eluents resulted in substantial lowering of the risk of contamination with extraneous Al [18][19][20][25][26][27][28][29]. Efforts were also oriented towards efficiently cleaning the chromatographic support of the column resins [18][19][20][27][28][29].…”

“…Different cleaning procedures of the eluents resulted in substantial lowering of the risk of contamination with extraneous Al [18][19][20][25][26][27][28][29]. Efforts were also oriented towards efficiently cleaning the chromatographic support of the column resins [18][19][20][27][28][29]. For speciation of Al bound to serum proteins by FPLC different eluents and various types of gradient elution were applied.…”

“…For speciation of Al bound to serum proteins by FPLC different eluents and various types of gradient elution were applied. Separation of proteins were obtained in 20 min [25,26,29] or in 50 min [27,28]. The chromatographic peaks were identified by UV detection and Al was determined ''off-line'' by ETAAS [25,29] or ''on-line'' by high resolution ICP-MS (HR-ICP-MS) [26][27][28].…”

Different Binding Affinities of Pb2+ and Cu2+ to Glycosylation Variants of Human Serum Transferrin Interfere with the Detection of Carbohydrate-Deficient Transferrin

“…Although different binding affinities of glycosylation variants to metal ions are observed (for example, Al 3+ binding to asialo-HTf is higher than that to native-HTf [26]), it is still unknown whether the CDT isoforms have higher binding affinities with heavy metal ions than the other glycosylation variants of HTf, and whether the heavy metal ions will interfere with CDT detection [27]. In our work, using UV-visible spectroscopy, fluorescence spectroscopy, ICP-MS, and isoelectric focusing (IEF), we focused on whether the metal ions Pb 2+ and Cu 2+ bound to holo-HTf and interfered with the detection of CDT.…”