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Quantitative bioanalysis using matrix‐assisted laser desorption/ionization mass spectrometry
Author(s) -
Jespersen S.,
Niessen W. M. A.,
Tjaden U. R.,
van der Greef J
Publication year - 1995
Publication title -
journal of mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 121
eISSN - 1096-9888
pISSN - 1076-5174
DOI - 10.1002/jms.1190300219
Subject(s) - chemistry , mass spectrometry , chromatography , internal standard , analyte , analytical chemistry (journal) , melittin , calibration curve , bioanalysis , matrix assisted laser desorption/ionization , quantitative analysis (chemistry) , desorption , matrix (chemical analysis) , detection limit , peptide , adsorption , biochemistry , organic chemistry
Abstract The application of matrix‐assisted laser desorption/ionization mass spectrometry (MALDI‐MS) for quantitative analysis was investigated with the use of internal standards. Three peptides/proteins in the mass range 1000–12000 were tested and the effect of various internal standards was evaluated. Horse cytochrome c was used as an internal standard for bovine cytochrome c , melittin for renin and an undecapeptide B analogue was employed as an internal standard for the decapeptide A. A linear response was found between the measured peak height ratio and the applied amount of analyte when an appropriate internal stanard was used. The quantitative abilities of MALDI‐MS were finally applied to the determination of the drug amperozide in plasma. The biological samples were prepared for analysis using liquid–liquid extraction prior to MALDI‐MS. A linear calibration graph was obtained using the 13 C 4 stable isotopically labelled amperozide as an internal standard.