Metal-binding proteins (MBPs) play an important role in physiology, fulfilling different functions such as regulation of the metal ion homeostasis, detoxification, participation in unspecific immuno-reactions, uptake, transport and storage of oxygen and regulation of gene expression. Some of the MBPs are crucial to achieve a healthy status. For instance, myoglobin can be used as indicator of heart infarction. Hemoglobin together with ferritin are very closely related to anaemia, the most common nutritional disease in the world. HbA1c is a glycated sub-isoform of hemoglobin and corresponds to the glucose concentration that was present in blood two or three months before the blood sampling. This glycated form can thus be used to control long-term glucose in the blood of patients with diabetes mellitus.

 To have access to this information, fundamental from the biochemical and medical point of view, reliable and performing analytical methods are needed for the MBP characterisation and quantification and for their monitoring. Within this frame, the paper will review the recent developments and trends in the field of MBP analysis using capillary electrophoretic (CE) methods. The emphasis will be put on several selected proteins which encompass albumin, aminopeptidase, carbonic anhydrase, conalbumin, cytochrome c, ferritin, glutathione peroxidase, hemoglobin, myoglobin, plasma amine oxidase, superoxide dismutase and transferrin.

The influence of major parameters in CE, particularly pH, will be commented. Recent results from our group will illustrate some optimised separations of the mentioned proteins.