Identification, characterization and determination of metal-binding proteins by liquid chromatography. A review

Abstract

The use of liquid chromatography in the separation and determination of metal-binding proteins is reviewed. Advantages and drawbacks of different chromatographic techniques based on various principles: size exclusion, ion exchange (cationic and ionic), reversed phase and affinity, are presented and discussed. The topic "metal-binding proteins" is considered and presented from two different points of view. The first one regards metal speciation in biological samples (serum and blood). In metal speciation studies, the exact identity of the protein to which the metal is bound often remains unknown. The second point of view is that, frequently, the interest of analyzing metal-binding proteins is not related anymore to the metallic fraction of the protein, but to other chemical structures attached to the protein, such as carbohydrates, which indirectly determine how good the function of the protein is. In this review, special attention is paid to studies dealing with the glycosylation of transferrin, and with the glycated isoform of haemoglobin.