Speciation of basal aluminium in human serum by fast protein liquid chromatography with inductively coupled plasma mass spectrometric detection

• Published in: Analyst (London) Vol. 123; no. 5; pp. 865 - 869
• Main Authors: BELEN SOLDADO CABEZUELO, A, MONTES BAYON, M, BLANCO GONZALEZ, E, GARCIA ALONSO, J. I, SANZ-MEDEL, A
• Format: Conference Proceeding Journal Article
• Language: English
• Published: Cambridge Royal Society of Chemistry 01.05.1998
• Subjects: Aluminum - blood; Aluminum - metabolism; Analytical, structural and metabolic biochemistry; Biological and medical sciences; Blood Proteins - metabolism; Chromatography, Liquid; Fundamental and applied biological sciences. Psychology; Humans; Inorganic compounds; Other biological molecules; Protein Binding; Spectrum Analysis; Human; Biological fluid; Coupled method; Serum; Aluminium; FPLC chromatography; Inductive coupling plasma spectrometry; Inorganic element; Mass spectrometry; Speciation
• ISSN: 0003-2654; 1364-5528
• DOI: 10.1039/a707669j

The coupling of fast protein liquid chromatography (FPLC) with inductively couples plasma mass spectrometry (ICP-MS) was evaluated as a technique for studying aluminium bound to proteins present in human serum. Separation of human serum proteins was achieved on a MonQ (HR5/5) anion-exchange column using an ammonium acetate gradient (0-0.25 mol I-1) at the physiological pH of 7.4 (0.05 mol l-1 TRIS-HC1 buffer). Aluminium contamination was avoided with an on-line Al-chelating scavenger column. Proteins were detected spectrophotometrically at 295 nm and the Al detection was carried out on-line using both quadrupole ICP-MS and double-focusing ICP-MS systems. At metal basal levels in serum the latter detector proved to be adequate for this detection. Results obtained with the procedure developed confirmed clearly that transferrin is the only significant A1-binding proteins in unspiked uraemic serum. In addition, a high-resolution ICP-MS instrument was applied successfully as an A1-specific detector allowing for the first time A1 speciation studies in unspiked normal serum. The technique can also be used for studying the protein binding of elements other than A1.