Immobilized metal ion affinity chromatography of serum albumins.
The interaction of several serum albumins with chelated (iminodiacetate, IDA) and immobilized (agarose-IDA) metal ions, Co2+, Ni2+, Cu2+ and Zn2+, was studied. There was no retention of human, bovine, porcine, murine and avian albumins on IDA-Zn(II) and IDA-Co(II) columns. However, all albumins studied, i.e., those of: man, cow, pig, dog, rabbit, rat, mouse, chicken and pigeon were retained on IDA-Cu(II) columns, and all except dog albumin were retained also on IDA-Ni(II). The recognition of albumins by chelated and immobilized transition metals seems to be related to an affinity for the imidazole side chains. It is postulated that one to three imidazoles is involved in this interaction, under the employed experimental conditions (pH 7.0; 1 M sodium chloride). There is no evidence for any significant contribution of tryptophan or cysteine (Cys 34) residues to the chromatographic event. The retention of defatted albumin and albumin oligomers (human), on IDA-Cu(II) columns was not significantly different from that of non-defatted albumin or albumin monomer, respectively.
Andersson
L
L
Institute of Biochemistry and Biochemical Separation Center, Uppsala University, Sweden.
Sulkowski
E
E
Porath
J
J
D000818:Animals; D002846:Chromatography, Affinity; D003545:Cysteine; D004285:Dogs; D006639:Histidine; D006801:Humans; D008670:Metals; D012709:Serum Albumin / Q000302:isolation & purification*; D012710:Serum Albumin, Bovine / Q000302:isolation & purification; D014364:Tryptophan
D008670:Metals; D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D006639:Histidine; D014364:Tryptophan; D003545:Cysteine