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Mouse cytochrome P450 subfamily 1A, 3A, 1E, 2C, 2D isoenzyme activities and corresponding contents were measured by means of triple quadrupole mass spectrometer in Multiple Reaction Monitoring mode (MRM). The technique was developed and tested on microsomes from control mouse and after induction with phenobarbital or methylcholanthrene. MRM allowed us to measure the content of individual P450 isoforms without using isotopic-labeled peptides or derivatization reagent. The results of modifying the content of certain P450 isoforms correlated with the change of enzymatic activity, defined by marker substrates.

The analysis of protein-protein interactions has the growing importance in modern proteomics. It is caused by necessity of in-depth functional study of proteins which, as a rule, operate in living systems due to each other interaction in the stable or dynamic protein complexes. In this review, the brief description and a comparative evaluation of most frequently used approaches in existing variety of protein interactomics methods are given.