An optimized procedure for the capture, fractionation and proteomic analysis of proteins using hydrogel nanoparticles

Adam Rainczuk, Katie Meehan, David Lawrence Steer, Peter G Stanton, David M Robertson, Andrew N Stephens

Research output: Contribution to journalArticleResearchpeer-review

Abstract

We have developed an optimized procedure using dual size exclusion / affinity hydrogel nanoparticles to capture and comparatively analyze low molecular mass proteins directly from biological samples. The method described facilitates charge and size-dependent protein binding, direct analysis by mass spectrometry or other means and is highly reproducible. A comparative analysis of the low molecular mass proteome of plasma following freeze-thaw immediately after venipuncture is used to illustrate proof-of-concept. The technique described is rapid and may be easily reproduced in any laboratory.
Original languageEnglish
Pages (from-to)332 - 336
Number of pages4
JournalProteomics
Volume10
DOIs
Publication statusPublished - 2010

Cite this

Rainczuk, Adam ; Meehan, Katie ; Steer, David Lawrence ; Stanton, Peter G ; Robertson, David M ; Stephens, Andrew N. / An optimized procedure for the capture, fractionation and proteomic analysis of proteins using hydrogel nanoparticles. In: Proteomics. 2010 ; Vol. 10. pp. 332 - 336.
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An optimized procedure for the capture, fractionation and proteomic analysis of proteins using hydrogel nanoparticles. / Rainczuk, Adam; Meehan, Katie; Steer, David Lawrence; Stanton, Peter G; Robertson, David M; Stephens, Andrew N.

In: Proteomics, Vol. 10, 2010, p. 332 - 336.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Meehan, Katie

AU - Steer, David Lawrence

AU - Stanton, Peter G

AU - Robertson, David M

AU - Stephens, Andrew N

PY - 2010

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AB - We have developed an optimized procedure using dual size exclusion / affinity hydrogel nanoparticles to capture and comparatively analyze low molecular mass proteins directly from biological samples. The method described facilitates charge and size-dependent protein binding, direct analysis by mass spectrometry or other means and is highly reproducible. A comparative analysis of the low molecular mass proteome of plasma following freeze-thaw immediately after venipuncture is used to illustrate proof-of-concept. The technique described is rapid and may be easily reproduced in any laboratory.

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