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Molecular & Cellular Proteomics 7:2410-2418, 2008.
© 2008 by The American Society for Biochemistry and Molecular Biology, Inc.

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Research

Investigating the Quantitative Nature of MALDI-TOF MS^*,S

Emília Szájli, Tamás Fehér and Katalin F. Medzihradszky^,¶,||

From the Proteomics Research Group and Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Temesvári körút 62, H-6726 Szeged, Hungary and ^¶ Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94143-0446

MALDI-TOF MS has been applied by several groups to relative quantitative measurements. At the same time, the non-quantitative character of this method has been widely reported. We conducted experiments to test the reliability of this technique for quantitation using the statistical method of inverse confidence limit calculation for the first time in this context. The relationship between relative intensities of known amounts of standard peptides and their concentration ratios was investigated. We found that the concentration ratios determined by relative intensity measurements were highly inaccurate and strongly influenced by the molecular milieu of the sample analyzed. Thus, we emphasize the necessity of using the sample itself for calibration. We also performed experiments using an isotope-labeled derivative of the analyte as an internal standard for calibration line generation. As expected, the use of such standard led to a dramatic increase in precision and a less pronounced improvement in accuracy. We recommend performing a similar statistical analysis as a demonstration of reliability for every system where MALDI-TOF MS is used for quantitative measurements.

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