New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins

T. Mehlman; M. Benjamin; D. Merhav; F. Osman; Y. Ben-Asouli; R. Goldshleger; S. Karlish; A. Shainskaya

New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins

T. Mehlman^*
, M. Benjamin
, D. Merhav
, F. Osman
, Y. Ben-Asouli
, R. Goldshleger
, S. Karlish
, A. Shainskaya

^*Corresponding author for this work

Research output: Contribution to conference › Paper › peer-review

Abstract

A method was developed for the analysis of electroeluted proteins from Coomassie-stained SDS polyacrylamide gels. The method was compatible with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of integral membrane protein. The key step in the method involved an exchange of SDS by NaDOC during protein precipitation and washing steps. The exchange of SDS was followed by mass spectrometric analysis. The method provided a sensitivity of 1 pmol for standard proteins loaded on a gel. The method was found to be compatible with ESI mass spectrometry for hydrophilic proteins.

Original language	English
Pages	207-208
Number of pages	2
State	Published - 2002
Externally published	Yes
Event	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: 2 Jun 2002 → 6 Jun 2002

Conference

Conference	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/Territory	United States
City	Orlando, FL
Period	2/06/02 → 6/06/02

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Mehlman, T., Benjamin, M., Merhav, D., Osman, F., Ben-Asouli, Y., Goldshleger, R., Karlish, S., & Shainskaya, A. (2002). New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins. 207-208. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Mehlman, T. ; Benjamin, M. ; Merhav, D. et al. / New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.2 p.

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title = "New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins",

abstract = "A method was developed for the analysis of electroeluted proteins from Coomassie-stained SDS polyacrylamide gels. The method was compatible with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of integral membrane protein. The key step in the method involved an exchange of SDS by NaDOC during protein precipitation and washing steps. The exchange of SDS was followed by mass spectrometric analysis. The method provided a sensitivity of 1 pmol for standard proteins loaded on a gel. The method was found to be compatible with ESI mass spectrometry for hydrophilic proteins.",

author = "T. Mehlman and M. Benjamin and D. Merhav and F. Osman and Y. Ben-Asouli and R. Goldshleger and S. Karlish and A. Shainskaya",

year = "2002",

language = "אנגלית",

pages = "207--208",

note = "Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics ; Conference date: 02-06-2002 Through 06-06-2002",

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Mehlman, T, Benjamin, M, Merhav, D, Osman, F, Ben-Asouli, Y, Goldshleger, R, Karlish, S & Shainskaya, A 2002, 'New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins', Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States, 2/06/02 - 6/06/02 pp. 207-208.

New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins. / Mehlman, T.; Benjamin, M.; Merhav, D. et al.
2002. 207-208 Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Research output: Contribution to conference › Paper › peer-review

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AU - Mehlman, T.

AU - Benjamin, M.

AU - Merhav, D.

AU - Osman, F.

AU - Ben-Asouli, Y.

AU - Goldshleger, R.

AU - Karlish, S.

AU - Shainskaya, A.

PY - 2002

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AB - A method was developed for the analysis of electroeluted proteins from Coomassie-stained SDS polyacrylamide gels. The method was compatible with matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of integral membrane protein. The key step in the method involved an exchange of SDS by NaDOC during protein precipitation and washing steps. The exchange of SDS was followed by mass spectrometric analysis. The method provided a sensitivity of 1 pmol for standard proteins loaded on a gel. The method was found to be compatible with ESI mass spectrometry for hydrophilic proteins.

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T2 - Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics

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ER -

Mehlman T, Benjamin M, Merhav D, Osman F, Ben-Asouli Y, Goldshleger R et al.. New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins. 2002. Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

New method for the analysis of electroeluted proteins from coomassie-stained SDS polyacrylamide gels compatible with matrix-assisted laser desorption/ionization mass spectrometry of integral membrane proteins

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