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It becomes increasingly clear that most proteins of living systems exist as components of various protein  complexes rather than individual molecules. The use of various proteomic techniques significantly extended  our knowledge not only about functioning of individual complexes but also formed a basis for systemic analysis  of protein-protein interactions. In this study gel-filtration chromatography accompanied by mass-spectrometry  was used for the interactome analysis of human liver proteins. In six fractions (with average molecular masses  of 45 kDa, 60 kDa, 85 kDa, 150 kDa, 250 kDa, and 440 kDa) 797 proteins were identified. In dependence of their  distribution profiles in the fractions, these proteins could be subdivided into four groups: (1) single monomeric proteins  that are not involved in formation of stable protein complexes; (2) proteins existing as homodimers or heterodimers  with comparable partners; (3) proteins that are partially exist as monomers and partially as components of protein  complexes; (4) proteins that do not exist in the monomolecular state, but also exist within protein complexes  containing three or more subunits. Application of this approach to known isatin-binding proteins resulted  in identification of proteins involved in formation of the homo- and heterodimers and mixed protein complexes.

The analysis of participation of individual proteins in the protein interactome formation