Quantification of target proteins using hydrogel antibody arrays and MALDI time-of-flight mass spectrometry (A2M2S)

Item Type:	Article
Title:	Quantification of target proteins using hydrogel antibody arrays and MALDI time-of-flight mass spectrometry (A2M2S)
Creators Name:	Darii, E. and Lebeau, D. and Papin, N. and Rubina, A.Y. and Stomakhin, A. and Tost, J. and Sauer, S. and Savvateeva, E. and Dementieva, E. and Zasedatelev, A. and Makarov, A.A. and Gut, I.G.
Abstract:	Mass spectrometry-based analysis techniques are widely applied in proteomics. This study presents a novel method for quantitative multiplex candidate protein profiling. It applies immunocapture of differentially labeled protein complements on hydrogel antibody arrays and subsequent quantification by MS. To make this approach quantitative a labeling approach was devised. The impact of labeling on the antibody/antigen interaction was assessed in detail by surface plasmon resonance. Owing to there solution by mass more than two protein samples can be compared simultaneously. Direct labeling of crude samples such as sera was developed and so enables the absolute quantification of target proteins straight from crude samples without a protein purification step. It was used to measure the concentration of apolipoprotein A-1 in serum. This method has been termed A2M2S for Affinity Array sand MALDI Mass Spectrometry.
Keywords:	Hydrogels, Immunoassay, Mass Spectrometry, Matrix-Assisted Laser Desorption-Ionization, Protein Array Analysis, Proteins, Proteomics
Source:	New Biotechnology
ISSN:	1871-6784
Publisher:	Elsevier
Volume:	25
Number:	6
Page Range:	404-416
Date:	15 September 2009
Official Publication:	https://doi.org/10.1016/j.nbt.2009.03.001
PubMed:	View item in PubMed

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