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The relationship between the amount of a target protein in a complex biological sample and its amount  measured by selected reaction monitoring (SRM) mass spectrometry upon the affinity enrichment of target protein with  aptamers immobilized on a solid phase was studied. Human thrombin added in known concentrations to cellular  extracts derived from bacterial cells was used as model target protein. It has been demonstrated that the affinity  enrichment of thrombin in cellular extracts by means of the thrombin-binding aptamer immobilized on the surface  of magnetic microbeads results in an approximately 10-fold increase of the concentration of target protein and  a 100-fold decrease of the low limit of a target protein concentration range where its quantitative detection by SRM  is possible without an interference from other peptides present in a tryptic digest.

Use of DNA-aptamers for enrichment of low abundant proteins in cellular extracts for quntitative detection by selected reaction monitoring