Scientific publications

Membrane protein profiling of human islets of Langerhans using several extraction methods

Clin. Proteom., 2010, 6(4), 195 - 207
Sara F. Hansson, Ã…sa Henriksson, Lars Johansson, Olle Korsgren, Jan W. Eriksson, Hans Tornqvist, Pia Davidsson

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Improving the depth of coverage in membrane proteomic studies through the use of lipid-based protein immobilization technology in parallel with methanol-facilitated solubilisation

Anal. Methods, 2010, 2, 539 - 545
Neerav D. Padliya, Mohit B. Bhatia, Wolfgang T. Hofgärtner and Robert J. Hariri

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Elucidation of the outer membrane proteome of Salmonella enterica serovar Typhimurium utilising a lipid-based protein immobilization technique

BMC Microbiol., 2010, 10, 44
Darren Chooneea, Roger Karlsson, Vesela Encheva, Cath Arnold, Hazel Appleton, and Haroun Shah

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Identification of key proteins involved in the anammox reaction

FEMS Microbiology Letters, 2009, 297(1), 87 - 94
Roger Karlsson, Anders Karlsson, Ola Bäckman, Bengt R. Johansson, Stefan Hulth

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Proteomic analysis of plasma membrane vesicles

Angew. Chem. Int. Ed. Engl., 2009, 48(9), 1656 - 1659
Bauer B, Davidson M, Orwar O

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Anal. Methods, 2010, 2, 539 - 545

Lipid-based protein immobilization (LPI) technology is a platform recently developed to facilitate shotgun membrane proteomic studies based on a nanotechnology framework. Proteoliposomes are generated from a membrane protein preparation. These proteoliposomes are immobilized onto an LPI chip and then subjected to proteolysis. The proteolytic peptides are then subjected to LC/MS analysis after fractionation by SCX chromatography. The focus of this study was to evaluate how the depth of coverage of the membrane proteome of a particular cell type varied as a function of the sample preparation method used. Human dermal fibroblasts (hDFs) and human bone marrow mesenchymal stem cells (BM-hMSCs) were subjected to membrane proteomic studies using two different sample preparation methods: LPI technology and methanol-facilitated solubilisation. The number of membrane proteins that could be identified from hDFs and BM-hMSCs using LC/MS was greater using LPI technology than it was using methanol-facilitated solubilisation. However, the number of membrane protein identifications that could be made for both hDFs and BM-hMSCs increased by 50% when both sample preparation methods were used in parallel and the MS/MS data was convolved together. Therefore, LPI technology is a very useful technology for high-throughput shotgun membrane proteomic studies. However, in order to maximize the depth of membrane proteome coverage that can be attained for a given cell type, it is necessary to use multiple sample preparation methods in concert.