Proteins perform several functions in living organisms, including catalytic reactions and transport of molecules or ions within the cells, the organs or the whole body. The understanding of the processes in human organisms, which are mainly driven by biochemical reactions and protein-protein interactions, depends to a great extent on the ability to isolate active proteins in biological samples for more detailed examination of chemical structure and physiological function. This essential information can imply an important indication of a patient's state of health.
As about 30–40% of all known proteins contain one or more metal ion cofactors (e.g., ceruloplasmin, ferritin, amyloid-beta precursor protein, matrix metalloproteinase, or metallochaperones), especially native and denatured metalloproteins have to be isolated, identified and quantified after liquid biopsy. Many of these cofactors  (e.g., iron, copper, or zinc) play a key role in vital enzymatic catalytic processes or stabilize globular protein molecules. Therefore, the high-precision gel electrophoresis and comparable separation techniques are highly relevant as initial step of protein and trace metal speciation analysis, subsequently, followed by modern mass spectrometric and magnetic resonance methods for quantifying and identifying the soluble proteins of interest.