Effect of impurities on the matrix‐assisted laser desorption/ionization mass spectra of insulin

Bajuk, Anna; Głuch, K.; Michalak, Leszek

doi:10.1002/rcm.521

Cited by 24 publications

(13 citation statements)

References 20 publications

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“…Various studies report in detail on the effect of various buffers and salts on the MALDI MS analysis of biopolymers such as proteins, peptides, and DNA (Mock, Sutton, & Cottrell, 1992;Kallweit et al, 1996;Shaler et al, 1996;Yao et al, 1998;Amini et al, 2000;Bajuk, Gluch, & Michalak, 2001). Such studies have not yet been performed for pharmaceutical compounds.…”

Section: B Ion Suppressionmentioning

confidence: 98%

Biomedical application of MALDI mass spectrometry for small‐molecule analysis

Kampen

Burgers

Groot

et al. 2010

Mass Spectrometry Reviews

139

102

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Matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is an emerging analytical tool for the analysis of molecules with molar masses below 1,000 Da; that is, small molecules. This technique offers rapid analysis, high sensitivity, low sample consumption, a relative high tolerance towards salts and buffers, and the possibility to store sample on the target plate. The successful application of the technique is, however, hampered by low molecular weight (LMW) matrix-derived interference signals and by poor reproducibility of signal intensities during quantitative analyses. In this review, we focus on the biomedical application of MALDI-MS for the analysis of small molecules and discuss its favorable properties and its challenges as well as strategies to improve the performance of the technique. Furthermore, practical aspects and applications are presented.

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Section: B Ion Suppressionmentioning

confidence: 98%

Biomedical application of MALDI mass spectrometry for small‐molecule analysis

Kampen

Burgers

Groot

et al. 2010

Mass Spectrometry Reviews

139

102

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“…Various papers describe the effects due to salts, buffers, and detergents (Shaler et al, 1996;Amini et al, 2000;Bajuk, Gluch, & Michalak, 2001). In particular, Bajuk, Gluch, & Michalak (2001) have measured the effect of contaminants such as sodium sulfate (Na 2 SO 4 ), copper sulfate (CuSO 4 ), potassium ferrocyanide (K 4 Fe(CN) 6 ), and triammonium citrate ((NH 4 ) 3 C 6 H 5 O 7 ) on the positive-ion MALDI-TOF spectra of insulin. 2,5-Dihydroxybenzoic acid was used as matrix, and the concentrations of different salts that reduce the insulin signal to zero were also determined.…”

Section: Problems With Buffersmentioning

confidence: 99%

Development of new methodologies for the mass spectrometry study of bioorganic macromolecules

Cristoni

Bernardi

2003

Mass Spectrometry Reviews

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I. Introduction 370 II. Techniques That Are Usually Employed in the Study of Bioorganic Macromolecules 371 A. Proteins and Peptides 371 B. Oligonucleotides 374 C. Oligosaccharides and Glycoconjugates 375 D. Various Complexes (DNA–Protein, Antigen–Antibody, Macromolecules–Metals) 377 III. Common Problems and Developments in the Analysis of Bioorganic Macromolecules by Mass Spectrometry 377 A. Ionization Source Problems and Developments 377 1. Sensitivity 377 2. Problems with Buffers 379 3. Multicharge Effect 381 B. Mass Analyzer Problems and Developments 381 1. Linear Dynamic Range 381 2. Tandem Mass Spectrometry 382 3. Sensitivity 382 4. Resolution 383 5. Mass Accuracy 383 IV. New Promising Technologies 384 A. Interfaces and Ionization Sources 384 1. Improvements in the Coupling of Liquid‐Phase Separation Systems to Mass Spectrometry 384 2. AP‐MALDI 384 3. Deprotonant Agents 385 4. Sonic Spray Ionization 388 5. APCI without Corona Discharge 391 B. Mass Analyzers 393 1. Linear Quadrupole Ion Trap 394 2. TOF Analyzers with New Detectors 395 3. Multiple Mass Analyzers 396 V. Software for Data Treatment 397 VI. Conclusions and Future Developments 399 Acknowledgments 400 References 400 In recent years, mass spectrometry has been increasingly used for the analysis of various macromolecules of biological, biomedical, and biochemical interest. This increase has been made possible by two key developments: the advent of electrospray ionization (ESI) and matrix‐assisted laser desorption ionization (MALDI) sources. The two new techniques produce a significant increase in mass range and in sensitivity that led to the development of new applications and of new analyzer designs, software, and robotics. This review, apart from the description of the status of mass spectrometry in the analysis of bioorganic macromolecules, is mainly devoted to the illustration of the more recent promising techniques and on their possible future evolution. © 2003 Wiley Periodicals, Inc., Mass Spec Rev 22:369–406, 2003; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/mas.10062

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“…Both electrospray ionization (ESI) [18] and matrix-assisted laser desorption/ionization (MALDI) [19] mass spectrometry have been applied for the analysis of GSLs [20][21][22][23]. MALDI MS can ionize GSLs even in the presence of contaminated substances, and the introduction of samples into the MS instrument is simpler in MALDI MS than in ESI MS [24][25][26]. However, it is difficult to identify individual molecular species by MS alone.…”

Section: Introductionmentioning

confidence: 99%

High-sensitivity analysis of glycosphingolipids by matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight imaging mass spectrometry on transfer membranes

Goto‐Inoue

Hayasaka

Sugiura

et al. 2008

Journal of Chromatography B

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Glycosphingolipids are ubiquitous constituents of cells. Yet there is still room for improvement in the techniques for analyzing glycosphingolipids. Here we report our highly sensitive and convenient analytical technology with imaging mass spectrometry for detailed structural analysis of glycosphingolipids. We were able to determine detailed ceramide structures; i.e. both the sphingosine base and fatty acid, by MS/MS/MS analysis on a PVDF membrane with 10 pmol of GM1, with which only faint bands were visible by primuline staining. The limit of detection was approximately 1 pmol of GM1, which is lower than the value in the conventional reports. (10 pmol)

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Effect of impurities on the matrix‐assisted laser desorption/ionization mass spectra of insulin

Cited by 24 publications

References 20 publications

Biomedical application of MALDI mass spectrometry for small‐molecule analysis

Biomedical application of MALDI mass spectrometry for small‐molecule analysis

Development of new methodologies for the mass spectrometry study of bioorganic macromolecules

High-sensitivity analysis of glycosphingolipids by matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight imaging mass spectrometry on transfer membranes

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