An optimized procedure for the capture, fractionation and proteomic analysis of proteins using hydrogel nanoparticles.
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 MS 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.
Rainczuk
Adam
A
Prince Henrys Institute of Medical Research, Clayton, VIC 3168, Australia.
Meehan
Katie
K
Steer
David L
DL
Stanton
Peter G
PG
Robertson
David M
DM
Stephens
Andrew N
AN
D001798:Blood Proteins / Q000032:analysis* / Q000737:chemistry; D002850:Chromatography, Gel / Q000379:methods*; D006801:Humans; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D040901:Proteomics / Q000379:methods*
D001798:Blood Proteins; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate