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Clinical Chemistry 31: 1969-1973, 1985;
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Clinical Chemistry, Vol 31, 1969-1973, Copyright © 1985 by American Association for Clinical Chemistry

Methods for studying the binding of aluminum by serum protein

H Rahman, AW Skillen, SM Channon, MK Ward and DN Kerr

We describe methods for studying the binding of Al by protein in serum: ultrafiltration, gel filtration, and immuno-affinity chromatography. For ultrafiltration we used an Amicon YM10 cellophane membrane with a nominal cutoff of 10 000 Da to separate ultrafiltrable and non- ultrafiltrable Al. For gel filtration we used Sephacryl S-300, and for immuno-affinity chromatography we used anti-transferrin coupled to CNBr- activated Sepharose to identify the Al-binding protein. For 30 normal subjects 54% of the total Al in serum was non-ultrafiltrable; for 30 patients with chronic renal failure being treated by hemodialysis 67% was non-ultrafiltrable. In both groups transferrin was identified as the major Al-binding protein in the serum. Results of gel-filtration studies should be interpreted with caution: some gel media adsorb "free" Al, which can be subsequently taken up by transferrin or desferrioxamine passing through the column. We find affinity chromatography to be a specific and reliable method, suitable for use in quantitative studies.


The following articles in journals at HighWire Press have cited this article:


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 Ann. N. Y. Acad. Sci.Home page
S. J. VAN RENSBURG, M. E. CARSTENS, F.C. V. POTOCNIK, and J.J. F. TALJAARD
The Effect of Iron and Aluminum on Transferrin and Other Serum Proteins as Revealed by Isoelectric Focusing Gel Electrophoresis
Ann. N.Y. Acad. Sci., April 1, 2000; 903(1): 150 - 155.
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 Clin. Chem.Home page
P. Menendez-Fraga, J. L. Fernandez-Martin, E. Blanco-Gonzalez, and J. B. Cannata-Andia
Low percentage of aluminoxamine and ferrioxamine in uremic serum after desferrioxamine administration
Clin. Chem., June 1, 1998; 44(6): 1262 - 1268.
[Abstract] [Full Text] [PDF]


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