Mass Spectrometry

Alongside our internationally-competitive research, the Babraham Institute maintains unique research facilities of national importance. The Mass Spectrometry facility has a range of mass spectrometers which can be used for the analysis of almost any type of biomolecule.

A recent investment of £1.5M by the BBSRC has enabled a significant enhancement of the facility with the purchase of several new mass spectrometers and ancillary equipment, including a Thermo LTQ Orbitrap Velos with ETD, two AB Sciex Qtrap 4000's, and a Thermo TSQ Quantum Ultra GC-MS.

Currently the work of the facility falls into two major areas, protein and lipid analysis, with dedicated instruments for specific analyses.

 

Protein Analysis

Mass spectrometers
Thermo LTQ Orbitrap Velos with ETD (NEW)
Applied Biosystems Voyager DE Pro MALDI-TOF
Applied Biosystems Q-Star ESI-Quadrupole-TOF

These instruments are mainly used for the identification, quantitation and detailed structural characterisation of proteins, and can be applied to purified proteins or complex mixtures.

Analyses include for example; identification of the components of protein complexes; identification and localisation of post-translational modifications (phosphorylation, ubiquitylation, glycosylation etc.); and quantitation of changes in the abundance of proteins (or modifications) resulting from specific biological processes.

 

Lipid Analysis

Mass spectrometers:
2 x AB Sciex Qtrap 4000 (NEW)
Thermo TSQ Quantum Ultra GC-MS (NEW)
Shimadzu IT-TOF

 

Recent Publications

Clark J, Anderson KE, Juvin V, Smith TS, Karpe F, Wakelam MJO, Stephens LR, Hawkins PT (2011)
Quantification of PtdInsP3 molecular species in cells and tissues by mass spectrometry.
Nature Methods
http://dx.doi.org/10.1038/nmeth.1564

 

Kilbey A, Terry A, Jenkins A, Borland G, Zhang Q, Wakelam MJO, Cameron ER, Neil JC (2010)
Runx regulation of sphingolipid metabolism and survival signalling.
Cancer Research 70 5860-5869
http://dx.doi.org/0.1158/0008-5472.CAN-10-0726

 

Hogan CJ, Aligianni S, Durand-Dubief M, Persson J, Will WR, Webster J, Wheeler L, Mathews CK, Elderkin S, Oxley D, Ekwall K, Varga-Weisz PD (2010)
Fission yeast Iec1-Ino80-mediated nucleosome eviction regulates nucleotide and phosphate metabolism.
Molecular and Cellular Biology 30 657-674
http://dx.doi.org/10.1128/MCB.01117-09

 

Corcos D, Osborn MJ, Matheson LS, Santos F, Zou X, Smith JA, Morgan G, Hutchings A, Hamon M, Oxley D, Bruggemann M (2010)
Immunoglobulin aggregation leading to Russell body formation is prevented by the antibody light chain.
Blood 115 282-288
http://dx.doi.org/10.1182/blood-2009-07-234864

 

Matheson LS, Osborn MJ, Smith JA, Corcos D, Hamon M, Chaouaf R, Coadwell WJ, Morgan G, Oxley D, Bruggemann M (2009)
Light chain-deficient mice produce novel multimeric heavy-chain-only IgA by faulty class switching.
International Immunology 21 957-966
http://dx.doi.org/10.1093/intimm/dxp062

 

Padinjat R, Coessens E, Manifava M, Georgiev P, Pettitt T, Wood E, Garcia-Murillas I, Okkenhaug H, Trivedi D, Zhang Q, Razzaq A, Zaid O, Wakelam MJO, O'Kane CJ, Ktistakis NT (2009)
Rhabdomere biogenesis in Drosophila photoreceptors is acutely sensitive to phosphatidic acid levels.
Journal of Cell Biology 185 129-145 (R Padinjat is cited as P Raghu)
http://dx.doi.org/10.1083/jcb.200807027

 

Young DS, Meersman F, Oxley D, Webster J, Gill AC, Bronstein I, Lowe CR, Dear DV (2009)
Effect of enzymatic deimination on the conformation of recombinant prion protein.
Biochimica et Biophysica Acta - Proteins and Proteomics 1794 1123-1133

http://dx.doi.org/10.1016/j.bbapap.2009.03.013

 

Jones R, James PS, Oxley D, Coadwell WJ, Suzuki-Toyota F, Howes EA (2008)
The equatorial subsegment in mammalian spermatozoa is enriched in tyrosine phosphorylated proteins.
Biology of Reproduction 79 421-431
http://dx.doi.org/10.1095/biolreprod.107.067314

 

Huang JT-J, Wang L, Prabakaran S, Wengenroth M, Lockstone HE, Koethe D, Gerth CW, Gross S, Schreiber D, Lilley K, Wayland M, Oxley D, Leweke FM, Bahn S (2008)
Independent protein-profiling studies show a decrease in apolipoprotein A1 levels in schizophrenia CSF, brain and peripheral tissues.
Molecular Psychiatry 13 1118-1128
http://dx.doi.org/10.1038/sj.mp.4002108

 

Zou X, Osborn MJ, Bolland DJ, Smith JA, Corcos D, Hamon M, Oxley D, Hutchings A, Morgan G, Santos F, Kilshaw PJ, Taussig MJ, Corcoran AE, Bruggemann M (2007)
Heavy chain-only antibodies are spontaneously produced in light chain-deficient mice.
Journal of Experimental Medicine 204 3271-3283
http://dx.doi.org/10.1084/jem.20071155

 

Dear DV, Young DS, Kazlauskaite J, Meersman F, Oxley D, Webster J, Pinheiro TJT, Gill AC, Bronstein I, Lowe CR (2007)
Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro.
Biochimica et Biophysica Acta - Proteins and Proteomics 1744 792-802
http://dx.doi.org/10.1016/j.bbapap.2007.05.005

 

Kulkarni S, Woollard KJ, Thomas S, Oxley D, Jackson SP (2007)
Conversion of platelets from a proaggregatory to a proinflammatory adhesive phenotype: role of PAF in spatially regulating neutrophil adhesion and spreading.
Blood 110 1879-1886
http://dx.doi.org/10.1182/blood-2006-08-040980

 

Zhao R, Oxley D, Smith TS, Follows GA, Green AR, Alexander DR (2007)
DNA damage-induced Bcl-xL deamidation is mediated by NHE-1 antiport regulated intracellular pH.
PLos Biology 5 e1, 39-53 (Online only)
http://dx.doi.org/10.1371/journal.pbio.0050001

 

Xia J, Sellers LA, Oxley D, Smith TS, Emson PC, Keverne EB (2006)
Urinary pheromones promote ERK/Akt phosphorylation, regeneration and survival of vomeronasal (V2R) neurons.
European Journal of Neuroscience 24 3333-3342
http://dx.doi.org/10.1111/j.1460-9568.2006.05244.x

 

Huang JT-J, Leweke FM, Oxley D, Wang L, Harris N, Koethe D, Gerth CW, Nolden BM, Gross S, Schreiber D, Reed B, Bahn S (2006)
Disease biomarkers in cerebrospinal fluid of patients with first-onset psychosis.
PLoS Medicine 3 e428, 2145-2158 (Online only)
http://dx.doi.org/10.1371/journal.pmed.0030428

 

Stirling FR, Cuzick A, Kelly SM, Oxley D, Evans TJ (2006)
Eukaryotic localization, activation and ubiquitinylation of a bacterial type III secreted toxin.
Cellular Microbiology 8 1294-1309
http://dx.doi.org/10.1111/j.1462-5822.2006.00710.x