Study of Non-Covalent Enzyme-Inhibitor Complexes of Aldose Reductase by Electrospray Mass Spectrometry
✍ Scribed by Noelle Potier; Patrick Barth; Denis Tritsch; Jean-François Biellmann; Alain Van Dorsselaer
- Book ID
- 115133690
- Publisher
- John Wiley and Sons
- Year
- 1997
- Tongue
- English
- Weight
- 996 KB
- Volume
- 243
- Category
- Article
- ISSN
- 1432-1327
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The recent development of electrospray ionization mass spectrometry (ESI-MS) has allowed its use to study molecular interactions driven by non-covalent forces. ESI-MS has been used to detect non-covalent complexes between proteins and metals, ligands and peptides and interactions involving DNA, RNA,
The detection of non-covalent complexes in the mass range 19 000-34 000 Da, using electrospray ionization mass spectrometry (ESI-MS), is reviewed. The examples discussed include (1) a protein-ligand interaction (ras-GDP), (2) an inhibitor-protein-ligand interaction (SCH 54292/SCH 54341-ras-GDP), (3)
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