Matrix-assisted laser desorption/ionization—boundary-activated dissociation of peptide ions in a quadrupole ion trap

Ray, Kenneth L.; Glish, Gary L.

doi:10.1016/s1387-3806(02)00807-2

Cited by 2 publications

(1 citation statement)

References 35 publications

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“…[25][26][27][28] Up to now, most ion trap instruments have been equipped with electrospray ionization (ESI) sources that provide a continuous ion beam which has been found beneficial for loading the ion trap with enough sample 29,30 Only recently, ion trap instruments were designed that allow the use of matrix-assisted laser desorption/ionization (MALDI) sources in order to deliver ion packages in a discontinuous mode. 28, [31][32][33] The advantageous features of the latter concept are (i) easy sample preparation and precursor ion creation, (ii) minimal sample consumption and (iii) real collision-induced dissociation (CID) conditions. These features are combined successfully in the matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight multiple-stage tandem mass spectrometry (MALDI-QIT-ToF-MS n ) instrument that was used in this study and enabled the determination of the amino acid sequences and structural details of haptoglobin proteins derived from human proteome samples.…”

Section: Introductionmentioning

confidence: 99%

Primary Structure Details of Haptoglobin α Chain Proteins from Human Plasma Samples are Resolved by Matrix-Assisted Laser Desorption/Ionization Quadrupole Ion Trap Time-of-Flight Multiple-Stage Tandem Mass Spectrometry Sequencing

Koy

Glocker²,

Resch

et al. 2004

Eur J Mass Spectrom (Chichester)

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MALDI QIT ToF MS(n) analyses lead to the rapid identification of protein structural details, as readily interpretable spectra after peptide fragmentations were obtained showing ion signals with high abundance even with sample amounts in the low femtomole range. In our studies we show that the Hp alpha 1F form that contained a C-terminal arginine residue was found to be the only contributing component to spot 149. By contrast, spots 77 and 79 were found to consist of two haptoglobin forms each. Spot 77 consists of Hp alpha 1S and deamidated Hp alpha 1F, whereas spot 79 consists of Hp alpha 1F and of Hp alpha 1S that contains a C- terminal arginine residue. The use of ion traps, enabling the acquisition of MSn spectra serves as a powerful peptide sequencing method for the analysis of both, genetic differences and post-translational modification events as the main reason for the observed spot pattern in the 2-D gels of haptoglobin proteins.

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Section: Introductionmentioning

confidence: 99%

Primary Structure Details of Haptoglobin α Chain Proteins from Human Plasma Samples are Resolved by Matrix-Assisted Laser Desorption/Ionization Quadrupole Ion Trap Time-of-Flight Multiple-Stage Tandem Mass Spectrometry Sequencing

Koy

Glocker²,

Resch

et al. 2004

Eur J Mass Spectrom (Chichester)

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Current literature in mass spectrometry

2003

J. Mass Spectrom.

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In order to keep subscribers up‐to‐date with the latest developments in their field, John Wiley & Sons are providing a current awareness service in each issue of the journal. The bibliography contains newly published material in the field of mass spectrometry. Each bibliography is divided into 11 sections: 1 Books, Reviews & Symposia; 2 Instrumental Techniques & Methods; 3 Gas Phase Ion Chemistry; 4 Biology/Biochemistry: Amino Acids, Peptides & Proteins; Carbohydrates; Lipids; Nucleic Acids; 5 Pharmacology/Toxicology; 6 Natural Products; 7 Analysis of Organic Compounds; 8 Analysis of Inorganics/Organometallics; 9 Surface Analysis; 10 Environmental Analysis; 11 Elemental Analysis. Within each section, articles are listed in alphabetical order with respect to author (5 Weeks journals ‐ Search completed at 19th. February. 2003)

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Matrix-assisted laser desorption/ionization—boundary-activated dissociation of peptide ions in a quadrupole ion trap

Cited by 2 publications

References 35 publications

Primary Structure Details of Haptoglobin α Chain Proteins from Human Plasma Samples are Resolved by Matrix-Assisted Laser Desorption/Ionization Quadrupole Ion Trap Time-of-Flight Multiple-Stage Tandem Mass Spectrometry Sequencing

Primary Structure Details of Haptoglobin α Chain Proteins from Human Plasma Samples are Resolved by Matrix-Assisted Laser Desorption/Ionization Quadrupole Ion Trap Time-of-Flight Multiple-Stage Tandem Mass Spectrometry Sequencing

Current literature in mass spectrometry

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