Sample-matrix preparation procedures are shown to greatly influence the quality of the matrix-assisted laser desorption/ionization (MALDI) mass spectra of peptides and proteins. In particular, dramatic mass discrimination effects are observed when using the matrix 4-hydroxy-?-cyanocinnamic acids for analyzing complex mixtures of peptides and proteins. The discrimination effects are found to be strongly dependent on the sample-matrix solution composition, pH, and the rates at which the sample-matrix co-crystals are grown. These findings demonstrate the need to exercise great care in performing and interpreting MALDI analysis of biological samples. The results also indicate that there is a chromatographic-like behavior in the sample-matrix preparation procedures that can be exploited to optimize the analysis. The present work describes the conditions under which the majority of components of a complex mixture of peptides and proteins can be successfully measured. A paper describing these results was published (S.L. Cohen and B.T. Chait, Anal. Chem. 68 (1996) 31-37.) We continue to investigate the influence of different sample preparation procedures on the information content in MALDI mass spectra and continue to make findings of practical importance

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR000862-27
Application #
6307586
Study Section
Project Start
1999-12-01
Project End
2000-11-30
Budget Start
1998-10-01
Budget End
1999-09-30
Support Year
27
Fiscal Year
2000
Total Cost
$8,199
Indirect Cost
Name
Rockefeller University
Department
Type
DUNS #
071037113
City
New York
State
NY
Country
United States
Zip Code
10065
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