| Literature DB >> 15792723 |
Sarah Trimpin1, Max L Deinzer.
Abstract
An efficient, low sample load mini-ball mill (MBM) sample preparation procedure was developed for solvent-free MALDI analysis of peptides and proteins. Picomole sample amounts can be handled conveniently, with 30 s grinding times being sufficient. Matrix purity and molar analyte/matrix ratios are not as critical as with methods employing solvent. Ammonium salt is employed for protonation of the peptide and suppression of sodiation. This strategy allows for peptide mapping and other biochemical manipulations to be performed prior to MBM sample preparation and mass analysis. The analysis of bovine serum albumin (66 kDa) yielded good results, indicating that higher molecular weight proteins are accessible. A semi-solvent-free strategy by the MBM sample preparation method is also described.Entities:
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Year: 2005 PMID: 15792723 DOI: 10.1016/j.jasms.2004.12.014
Source DB: PubMed Journal: J Am Soc Mass Spectrom ISSN: 1044-0305 Impact factor: 3.109