Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1196028 | Journal of the American Society for Mass Spectrometry | 2007 | 4 Pages |
Abstract
Buffers and detergents are notorious for suppression of analyte signal in electrospray and MALDI mass spectrometry and, invariably, analysts will take steps to remove these contaminants before MS analysis. However, we have found serendipitously that protein signal with MALDI MS is improved by about an order of magnitude on the addition of small amounts of Tween80. Four charged states of BSA could easily be seen at less than 125 fmol/spot and with mixture of three proteins (BSA, trypsinogen, and protein A) the molecular ions could be detected on as little as 12.5 fmol of spotted material (per protein) using an automated laser firing sequence.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Craig S. Brinkworth, David J. Bourne,