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Quantification of membrane proteins using nonspecific protease digestions.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2009 (English)In: Journal of proteome research, ISSN 1535-3907, Vol. 8, no 12, 5666-73 p.Article in journal (Refereed) Published
Abstract [en]

We present a mass spectrometry-based method for the identification and quantification of membrane proteins using the low-specificity protease Proteinase K, at very high pH, to digest proteins isolated by a modified SDS-PAGE protocol. The resulting peptides are modified with a fragmentation-directing isotope labeled tag. We apply the method to quantify differences in membrane protein expression of Bacillus subtilis grown in the presence or absence of glucose.

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2009. Vol. 8, no 12, 5666-73 p.
URN: urn:nbn:se:su:diva-35469DOI: 10.1021/pr900741tISI: 000272339100026PubMedID: 19845334OAI: diva2:287380
Available from: 2010-01-18 Created: 2010-01-18 Last updated: 2010-12-27Bibliographically approved

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Bendz, Maria
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Department of Biochemistry and Biophysics

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