Mass Spectrometry

Mass spectrometry (MS) is now the central tool for high sensitivity and high throughput protein identification. By analysing small peptide fragments and determining their mass it is often possible to obtain good identification of the parent protein. This is particularly true for proteins extracted from two-dimensional gels (2DE) and is usually performed using Matrix Assisted Laser Desorption Ionisation (MALDI-TOF) mass spectrometers.

Proteome Sciences provides specialist skills and protocols from its mass spectrometry groups for bespoke analyses, discovery, characterisation and quantitation of novel post-translational modifications (PTMs) of proteins. These advanced technical capabilities have been successfully applied to the study of PTMs such as phosphorylation, glycosylation and ubiquitination, all of which are key biological processes across a broad range of human diseases.

For gel-free proteomics, and in cases where proteins from 2DE cannot be identified using MALDI-TOF, we use a combination of liquid chromatography and electrospray mass spectrometry LC/MS, Q-TOF and LC-Q. Here peptides in a complex mixture are first separated using ion exchange and reverse phase chromatography and are eluted directly into the mass spectrometer. The mass of each peptide is determined, and if necessary a second high energy ion beam can be used to break each peptide into its constituent amino acids to generate sequence tags.

SELDI-MS is used as an alternative means of profiling protein expression mainly in body fluids by isolating the molecules on a variety of protein microarrays.

Proteome Sciences plc is actively involved in research projects addressing a broad range of disease areas and has leading edge capability for protein separation, mass spectrometry and bioinformatics in human disease applications.

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