Never like today have proteomic
and glycoproteomic procedures been used as valuable tools to obtain information
and characterize general or specific proteomes such in disease states and todiscover disease biomarkers that can help in the diagnosis, prognosis and
treatment monitoring of several diseases, for instance in cancer.
Plasma and serum are the most
informative samples for proteomic studies but they are also the most difficult
versions of the human proteome, due to the high heterogeneity they present. The
complexity of these samples is potentiated by plasma or serum proteolysis, the
presence of protein and glycoprotein isoforms and post-translational
modifications of proteins. Additionally, the dynamic range of protein abundance
in these samples is very wide (in plasma the dynamic range comprises up to ten
orders of magnitude) and cannot be covered by a single analytical technique
without fractionation, depletion or concentration. Furthermore, disease
biomarkers occur in very low concentrations, at least in early stages, and the
analytical techniques must present adequate sensitivity to detect lowabundant
proteins or glycoproteins.(Read More)
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