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

K. G. Ptitsyn | Zendy; Светлана Новикова | Zendy; Y.Y. Kiseleva | Zendy; Alexander Moysa | Zendy; Leonid K. Kurbatov | Zendy; Tatiana Farafonova | Zendy; Sergey P. Radko | Zendy; Victor G. Zgoda | Zendy; Alexander I. Archakov | Zendy

Open Access

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

Author(s) -

K. G. Ptitsyn,

Светлана Новикова,

Y.Y. Kiseleva,

Alexander Moysa,

Leonid K. Kurbatov,

Tatiana Farafonova,

Sergey P. Radko,

Victor G. Zgoda,

Alexander I. Archakov

Publication year - 2018

Publication title -

biomeditsinskaya khimiya

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.192

H-Index - 15

eISSN - 2310-6972

pISSN - 2310-6905

DOI - 10.18097/pbmc20186401005

Subject(s) - aptamer , chemistry , thrombin , detection limit , target protein , chromatography , mass spectrometry , dna , selected reaction monitoring , biochemistry , tandem mass spectrometry , microbiology and biotechnology , platelet , biology , gene , immunology

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.

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