| Autor: |
Stephen M. Gómez, Cameron B. Gundersen, Kym F. Faull, Julian P. Whitelegge |
| Rok vydání: |
1998 |
| Předmět: |
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| Zdroj: |
Photosynthesis: Mechanisms and Effects ISBN: 9780792355472 |
| DOI: |
10.1007/978-94-011-3953-3_1014 |
| Popis: |
The ideal analysis of any protein includes a mass spectrum of the intact molecule to define the native covalent state and its heterogeneity. A versatile procedure for effective electrospray-ionization mass spectrometry (ESI-MS) of intact intrinsic membrane proteins purified using reverse-phase chromatography in aqueous formic acid/isopropanol has been developed (1). The spectra of spinach DI and D2 as well as bacteriorhodopsin achieved mass measurements that were within 0.01% of calculated theoretical values, setting a benchmark standard for analysis of such molecules (1). Typically, genome data needs manipulation before agreement with calculated masses is achieved. DNA sequencing errors, post-transcriptional, post-translational modifications as well as protein damage must all be considered. Spectra frequently reveal lesser quantities of other molecular species that can usually be equated with covalently modified sub-populations of the dominant proteins. Here we present spectra of the larger Photosystem 2 (PS2) subunits from pea illustrating the accuracy and resolution afforded by ESI-MS. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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