Conference proceeding
High Fidelity for Intact Analysis of Hydrophobic Proteins
55th ASMS Conference Proceedings
01/01/2007
Abstract
Ligand gated ion channels are multiunit receptors with allelic forms that differ in physiological function and anatomic distribution. In fact, the distribution of certain ion channels is known to be affected dynamically within a single cell by post translational modifications. Hence, the intact mass spectra of membrane proteins, which define their covalent modification status and heterogeneity, can be essential to elucidating receptor function. Unfortunately, MS-incompatible detergents such as SDS, CHAPS and NP-40 are usually required to maintain lipophilic proteins in solution. We have described a simple procedure that removes incompatible buffer components prior to intact analysis and peptide mapping by MALDI-TOF. Here we extend the study to RP-ESI of complex membrane mixtures.
Details
- Title: Subtitle
- High Fidelity for Intact Analysis of Hydrophobic Proteins
- Creators
- Mahbod HajivandiXiquan LiangPaul PredkiMarshall Pope
- Resource Type
- Conference proceeding
- Publication Details
- 55th ASMS Conference Proceedings
- Language
- English
- Date published
- 01/01/2007
- Academic Unit
- Medicine Administration
- Record Identifier
- 9984632132102771
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