Matrix‐assisted laser desorption of peptides and proteins on a quadrupole ion trap mass spectrometer
Abstract The use of ultraviolet matrix‐assisted laser desorption (MALD) to ionize peptides for analysis in a quadrupole ion trap is described. An ion source was modified to accommodate a fiber optic to transmit laser radiation from a notrogen laser (337 nm) to the tip of the sample probe containing...
| Published in: | Rapid Communications in Mass Spectrometry |
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| Main Authors: | , , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1993
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1002/rcm.1290070106 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Frcm.1290070106 https://onlinelibrary.wiley.com/doi/full/10.1002/rcm.1290070106 |
| Summary: | Abstract The use of ultraviolet matrix‐assisted laser desorption (MALD) to ionize peptides for analysis in a quadrupole ion trap is described. An ion source was modified to accommodate a fiber optic to transmit laser radiation from a notrogen laser (337 nm) to the tip of the sample probe containing peptide of protein samples in a matrix of 2,5‐dihydroxybenzoic acid (DHB) or 3,4‐dimethoxy‐4‐hydrexy‐cinnamic acid. Detection limits are demonstrated with 10 fmol of sperm‐whale‐myoglobin. The dimer of sperm‐whale myoglobin was also observed at m / z 34, 430. A. comparison is made of the tandem mass spectrum of (MS/MS) of human angiotensin I desorbed by MALD to that of the peptide desorbed by liquid secondary‐ion mass spectrometry. Both spectra were found to contain abundant structural information. |
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