Format

Send to

Choose Destination
See comment in PubMed Commons below
BMC Res Notes. 2012 Nov 1;5:612. doi: 10.1186/1756-0500-5-612.

An automated plasma protein fractionation design: high-throughput perspectives for proteomic analysis.

Author information

1
Institute of Clinical Physiology-CNR, Via Moruzzi 1, 56124 Pisa, Italy.

Abstract

BACKGROUND:

Human plasma, representing the most complete record of the individual phenotype, is an appealing sample for proteomics analysis in clinical applications. Up to today, the major obstacle in a proteomics study of plasma is the large dynamic range of protein concentration and the efforts of many researchers focused on the resolution of this important drawback.

FINDINGS:

In this study, proteins from pooled plasma samples were fractionated according to their chemical characteristics on a home-designed SPE automated platform. The resulting fractions were digested and further resolved by reversed-phase liquid chromatography coupled with MALDI TOF/TOF mass spectrometry. A total of 712 proteins were successfully identified until a concentration level of ng/mL. Pearson correlation coefficient was used to test reproducibility.

CONCLUSIONS:

Our multidimensional fractionation approach reduced the analysis time (2 days are enough to process 16 plasma samples filling a 96-well plate) over the conventional gel-electrophoresis or multi-LC column based methods. The robotic processing, avoiding contaminants or lack of sample handling skill, promises highly reproducible specimen analyses (more than 85% Pearson correlation). The automated platform here presented is flexible and easily modulated changing fractioning elements or detectors.

PMID:
23116412
PMCID:
PMC3517536
DOI:
10.1186/1756-0500-5-612
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for BioMed Central Icon for PubMed Central
    Loading ...
    Support Center