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Journal articles on the topic 'Mass spectrometry'

Author: Grafiati

Published: 4 June 2021

Last updated: 16 November 2024

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1

KASAMA, Takeshi. "Biological Mass Spectrometry. Quadrupole Mass Spectrometer." Journal of the Mass Spectrometry Society of Japan 44, no. 3 (1996): 393–405. http://dx.doi.org/10.5702/massspec.44.393.

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2

Glish, Gary L., and David J. Burinsky. "Hybrid mass spectrometers for tandem mass spectrometry." Journal of the American Society for Mass Spectrometry 19, no. 2 (February 2008): 161–72. http://dx.doi.org/10.1016/j.jasms.2007.11.013.

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3

Busch, Kenneth L., Gary L. Glish, Scott A. McLuckey, and John J. Monaghan. "Mass spectrometry/mass spectrometry: techniques and applications of tandem mass spectrometry." Analytica Chimica Acta 237 (1990): 509. http://dx.doi.org/10.1016/s0003-2670(00)83956-2.

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4

Futrell, Jean H. "Mass spectrometry/mass spectrometry: Techniques and applications of tandem mass spectrometry." Microchemical Journal 41, no. 2 (April 1990): 246–47. http://dx.doi.org/10.1016/0026-265x(90)90124-n.

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5

Moriarty, F. "Mass spectrometry/mass spectrometry. Techniques and applications of tandem mass spectrometry." Environmental Pollution 61, no. 3 (1989): 261. http://dx.doi.org/10.1016/0269-7491(89)90246-7.

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6

Cooks, R. G. "Mass Spectrometry/Mass Spectrometry. Techniques and Applications of Tandem Mass Spectrometry." International Journal of Mass Spectrometry and Ion Processes 93, no. 2 (October 1989): 265–66. http://dx.doi.org/10.1016/0168-1176(89)80103-x.

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7

Pinkston, J. David, Martin Rabb, J. Throck Watson, and John Allison. "New time‐of‐flight mass spectrometer for improved mass resolution, versatility, and mass spectrometry/mass spectrometry studies." Review of Scientific Instruments 57, no. 4 (April 1986): 583–92. http://dx.doi.org/10.1063/1.1138874.

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8

Glish, Gary L., and Scott A. McLuckey. "Hybrid Instruments for Mass Spectrometry/Mass Spectrometry." Instrumentation Science & Technology 15, no. 1 (January 1986): 1–36. http://dx.doi.org/10.1080/10739148608543593.

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9

Charles, M. Judith, and Yves Tondeur. "Choosing between high-resolution mass spectrometry and mass spectrometry/mass spectrometry environmental applications." Environmental Science & Technology 24, no. 12 (December 1990): 1856–60. http://dx.doi.org/10.1021/es00082a011.

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10

KONDO, Fumio, and Ken-ichi HARADA. "Biological Mass Spectrometry. Mass Spectrometric Analysis of Cyanobacterial Toxins." Journal of the Mass Spectrometry Society of Japan 44, no. 3 (1996): 355–76. http://dx.doi.org/10.5702/massspec.44.355.

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11

Wu, Junhan, Wenpeng Zhang, and Zheng Ouyang. "On-Demand Mass Spectrometry Analysis by Miniature Mass Spectrometer." Analytical Chemistry 93, no. 15 (April 5, 2021): 6003–7. http://dx.doi.org/10.1021/acs.analchem.1c00575.

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12

NOHMI, Takashi, and Tetsuya MIYAGISHI. "Future Mass from Miniaturized Mass Spectrometry to Micro Mass Spectrometry." Journal of the Mass Spectrometry Society of Japan 51, no. 1 (2003): 54–66. http://dx.doi.org/10.5702/massspec.51.54.

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13

Guerrera, Ida Chiara, and Oliver Kleiner. "Application of Mass Spectrometry in Proteomics." Bioscience Reports 25, no. 1-2 (February 4, 2005): 71–93. http://dx.doi.org/10.1007/s10540-005-2849-x.

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Mass spectrometry has arguably become the core technology in proteomics. The application of mass spectrometry based techniques for the qualitative and quantitative analysis of global proteome samples derived from complex mixtures has had a big impact in the understanding of cellular function. Here, we give a brief introduction to principles of mass spectrometry and instrumentation currently used in proteomics experiments. In addition, recent developments in the application of mass spectrometry in proteomics are summarised. Strategies allowing high-throughput identification of proteins from highly complex mixtures include accurate mass measurement of peptides derived from total proteome digests and multidimensional peptide separations coupled with mass spectrometry. Mass spectrometric analysis of intact proteins permits the characterisation of protein isoforms. Recent developments in stable isotope labelling techniques and chemical tagging allow the mass spectrometry based differential display and quantitation of proteins, and newly established affinity procedures enable the targeted characterisation of post-translationally modified proteins. Finally, advances in mass spectrometric imaging allow the gathering of specific information on the local molecular composition, relative abundance and spatial distribution of peptides and proteins in thin tissue sections.

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14

Termopoli, Veronica, Maurizio Piergiovanni, Davide Ballabio, Viviana Consonni, Emmanuel Cruz Muñoz, and Fabio Gosetti. "Condensed Phase Membrane Introduction Mass Spectrometry: A Direct Alternative to Fully Exploit the Mass Spectrometry Potential in Environmental Sample Analysis." Separations 10, no. 2 (February 17, 2023): 139. http://dx.doi.org/10.3390/separations10020139.

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Membrane introduction mass spectrometry (MIMS) is a direct mass spectrometry technique used to monitor online chemical systems or quickly quantify trace levels of different groups of compounds in complex matrices without extensive sample preparation steps and chromatographic separation. MIMS utilizes a thin, semi-permeable, and selective membrane that directly connects the sample and the mass spectrometer. The analytes in the sample are pre-concentrated by the membrane depending on their physicochemical properties and directly transferred, using different acceptor phases (gas, liquid or vacuum) to the mass spectrometer. Condensed phase (CP) MIMS use a liquid as a medium, extending the range to new applications to less-volatile compounds that are challenging or unsuitable to gas-phase MIMS. It directly allows the rapid quantification of selected compounds in complex matrices, the online monitoring of chemical reactions (in real-time), as well as in situ measurements. CP-MIMS has expanded beyond the measurement of several organic compounds because of the use of different types of liquid acceptor phases, geometries, dimensions, and mass spectrometers. This review surveys advancements of CP-MIMS and its applications to several molecules and matrices over the past 15 years.

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15

ITO, Yuji, and Masahiro MATSUI. "Mass Spectrometry." Journal of the Japan Society of Colour Material 63, no. 7 (1990): 419–29. http://dx.doi.org/10.4011/shikizai1937.63.419.

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16

Lederman, Lynne. "Mass Spectrometry." BioTechniques 46, no. 6 (May 2009): 399–401. http://dx.doi.org/10.2144/000113165.

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17

Yates, John R. "Mass spectrometry." Trends in Genetics 16, no. 1 (January 2000): 5–8. http://dx.doi.org/10.1016/s0168-9525(99)01879-x.

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18

Burlingame, A. L., D. S. Millington, D. L. Norwood, and D. H. Russell. "Mass spectrometry." Analytical Chemistry 62, no. 12 (June 15, 1990): 268–303. http://dx.doi.org/10.1021/ac00211a020.

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19

Burlingame, A. L., D. Maltby, D. H. Russell, and P. T. Holland. "Mass spectrometry." Analytical Chemistry 60, no. 12 (June 15, 1988): 294–342. http://dx.doi.org/10.1021/ac00163a021.

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20

Burlingame, A. L., Robert K. Boyd, and Simon J. Gaskell. "Mass Spectrometry." Analytical Chemistry 68, no. 12 (January 1996): 599–652. http://dx.doi.org/10.1021/a1960021u.

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21

Burlingame, A. L., Robert K. Boyd, and Simon J. Gaskell. "Mass Spectrometry." Analytical Chemistry 70, no. 16 (August 1998): 647–716. http://dx.doi.org/10.1021/a1980023+.

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22

Burlingame, A. L., T. A. Baillie, and D. H. Russell. "Mass spectrometry." Analytical Chemistry 64, no. 12 (June 15, 1992): 467–502. http://dx.doi.org/10.1021/ac00036a025.

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23

Kinter, Michael. "Mass spectrometry." Analytical Chemistry 67, no. 12 (June 15, 1995): 493–97. http://dx.doi.org/10.1021/ac00108a034.

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24

Caprioli, Richard, and Alan Wu. "Mass Spectrometry." Analytical Chemistry 65, no. 12 (June 15, 1993): 470–74. http://dx.doi.org/10.1021/ac00060a619.

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25

Burlingame, A. L., Robert K. Boyd, and Simon J. Gaskell. "Mass Spectrometry." Analytical Chemistry 66, no. 12 (June 1994): 634–83. http://dx.doi.org/10.1021/ac00084a024.

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26

Burlingame, A. L., Thomas A. Baillie, and Peter J. Derrick. "Mass spectrometry." Analytical Chemistry 58, no. 5 (April 1986): 165–211. http://dx.doi.org/10.1021/ac00296a015.

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27

Grotemeyer, Jürgen, Klaus G. Heumann, and Wolf D. Lehmann. "Mass spectrometry." Analytical and Bioanalytical Chemistry 386, no. 1 (August 8, 2006): 21–23. http://dx.doi.org/10.1007/s00216-006-0653-5.

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28

Van Thuijl, J. "Mass spectrometry." TrAC Trends in Analytical Chemistry 5, no. 3 (March 1986): IX—X. http://dx.doi.org/10.1016/0165-9936(86)85017-8.

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29

Grotemeyer, J. "Mass spectrometry." Analytical and Bioanalytical Chemistry 377, no. 7-8 (December 1, 2003): 1097. http://dx.doi.org/10.1007/s00216-003-2292-4.

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30

Vickerman, J. C. "Mass spectrometry." Endeavour 11, no. 2 (January 1987): 108. http://dx.doi.org/10.1016/0160-9327(87)90265-1.

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31

Jannetto, Paul J., and Darlington Danso. "Mass spectrometry." Clinical Biochemistry 82 (August 2020): 1. http://dx.doi.org/10.1016/j.clinbiochem.2020.06.003.

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32

P, D. "Mass Spectrometry." Journal of Molecular Structure 160, no. 1-2 (August 1987): 183. http://dx.doi.org/10.1016/0022-2860(87)87016-3.

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33

Robinson, Carol, and Robert J. Cotter. "Mass spectrometry." Proteins: Structure, Function, and Genetics 33, S2 (1998): 1–2. http://dx.doi.org/10.1002/(sici)1097-0134(1998)33:2+<1::aid-prot1>3.0.co;2-m.

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34

Lhotka, Radek, and Petr Vodička. "Aerosol Mass Spectrometry." Chemické listy 118, no. 5 (May 15, 2024): 254–62. http://dx.doi.org/10.54779/chl20240254.

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Mass spectrometry is widely used in various scientific fields. In atmospheric chemistry, there has been a long call for a detailed on-line analysis of the chemical composition of aerosol particles (i.e., particles in the solid or liquid state) in the atmosphere resulting in the development of the so-called aerosol mass spectrometers in the past 20 years. These instruments allow the measurement of the chemical composition of particles with sizes of ca. 50–800 nm, typically at minute resolution. Their development and possible applications are discussed in this review.

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35

NAGAO, Keisuke. "Fundamentals of Mass Spectrometry -Isotope Ratio Mass Spectrometry-." Journal of the Mass Spectrometry Society of Japan 59, no. 2 (2011): 35–49. http://dx.doi.org/10.5702/massspec.59.35.

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36

Musselman, Brian D. "K. Busch, G. Glish and S. Mcluckey. Mass spectrometry/mass spectrometry: Techniques and applications of tandem mass spectrometry, VCH publishing, New York, 1988. Mass Spectrometry/Mass Spectrometry." Biological Mass Spectrometry 18, no. 10 (October 1989): 942. http://dx.doi.org/10.1002/bms.1200181017.

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37

LaiHing, K., P. Y. Cheng, T. G. Taylor, K. F. Willey, M. Peschke, and M. A. Duncan. "Photodissociation in a reflectron time-of-flight mass spectrometer: a novel mass spectrometry/mass spectrometry configuration for high-mass systems." Analytical Chemistry 61, no. 13 (July 1989): 1458–60. http://dx.doi.org/10.1021/ac00188a031.

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38

Dogra, Akshay. "A Thorough Examination of the Recent Advances in Mass Spectrometry." International Journal for Research in Applied Science and Engineering Technology 11, no. 7 (July 31, 2023): 1731–41. http://dx.doi.org/10.22214/ijraset.2023.54964.

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Abstract: Mass spectrometry has become an essential tool in pharmaceutical analysis, revolutionizing drug development, quality assurance, and our understanding of complex biological systems. This review provides a comprehensive overview of recent advances in mass spectrometry for pharmaceutical analysis. We discuss the fundamentals of mass spectrometry, including ionization and mass analysis principles, as well as the various types of mass spectrometers used in pharmaceutical analysis. We explore high-resolution mass spectrometry (HRMS), tandem mass spectrometry (MS/MS), ambient ionization mass spectrometry, and mass spectrometry imaging (MSI), highlighting their applications in drug characterization, quantification, imaging, and biomarker discovery. Furthermore, we examine the challenges faced by mass spectrometry, such as matrix effects and data interpretation, and discuss emerging trends and future perspectives. By understanding the recent advancements and addressing the challenges, mass spectrometry can continue to drive advancements in pharmaceutical analysis and quality assurance

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39

Meier, Heiko, and Gottfried Blaschke. "Capillary electrophoresis–mass spectrometry, liquid chromatography–mass spectrometry and nanoelectrospray-mass spectrometry of praziquantel metabolites." Journal of Chromatography B: Biomedical Sciences and Applications 748, no. 1 (October 2000): 221–31. http://dx.doi.org/10.1016/s0378-4347(00)00397-2.

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40

Cooks, R. G., K. A. Cox, and J. D. Williams. "High-performance mass spectrometry with the ion trap mass spectrometer." Journal of Protein Chemistry 11, no. 4 (August 1992): 376–77. http://dx.doi.org/10.1007/bf01673733.

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41

Budzikiewicz, H. "Selected reviews on mass spectrometric topics. XXVIII. Tandem mass spectrometry." Mass Spectrometry Reviews 8, no. 2 (March 1989): 119. http://dx.doi.org/10.1002/mas.1280080204.

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42

Budzikiewicz, H. "Selected reviews on mass spectrometric topics. XLV. Pyrolysis-mass spectrometry." Mass Spectrometry Reviews 11, no. 3 (May 1992): 247. http://dx.doi.org/10.1002/mas.1280110304.

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43

Budzikiewicz, H. "Selected reviews on mass spectrometric topics. XLVII. Accelerator mass spectrometry." Mass Spectrometry Reviews 11, no. 5 (September 1992): 445. http://dx.doi.org/10.1002/mas.1280110505.

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44

Roberts, Norman B., Brian N. Green, and Michael Morris. "Potential of electrospray mass spectrometry for quantifying glycohemoglobin." Clinical Chemistry 43, no. 5 (May 1, 1997): 771–78. http://dx.doi.org/10.1093/clinchem/43.5.771.

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Abstract An electrospray ionization–mass spectrometric procedure has been developed for determining glycohemoglobin. Whole-blood samples from 78 diabetic and 50 nondiabetic subjects (glycation range 3–15%, as determined by electrospray mass spectrometry) were diluted 500-fold in an acidic denaturing solvent and introduced directly into a mass spectrometer. The resulting mass spectra were then processed to estimate the percentage of glycohemoglobin present in the sample. Total analysis time, including plotting the spectra and computing the percentage of glycation, was ∼3 min. The imprecision (CV) of the method was <5.1% for inter- and intrabatch analyses for total glycohemoglobin in the range 3.6–14%. Comparison of the mass spectrometric results with those from established affinity chromatographic procedures showed good overall agreement. The relative glycation of the α- and β-chains was determined directly and was shown to be constant (0.64:1) over the glycation range measured. Only single glucose attachment to both the α- and β-chains was observed.

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45

Tian, Qingguo, and Steven J. Schwartz. "Mass Spectrometry and Tandem Mass Spectrometry of Citrus Limonoids." Analytical Chemistry 75, no. 20 (October 2003): 5451–60. http://dx.doi.org/10.1021/ac030115w.

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46

Shoji, Yuki, Mari Yotsu-Yamashita, Teruo Miyazawa, and Takeshi Yasumoto. "Electrospray Ionization Mass Spectrometry of Tetrodotoxin and Its Analogs: Liquid Chromatography/Mass Spectrometry, Tandem Mass Spectrometry, and Liquid Chromatography/Tandem Mass Spectrometry." Analytical Biochemistry 290, no. 1 (March 2001): 10–17. http://dx.doi.org/10.1006/abio.2000.4953.

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47

Cooks, R. Graham, Alan K. Jarmusch, Christina R. Ferreira, and Valentina Pirro. "Skin molecule maps using mass spectrometry." Proceedings of the National Academy of Sciences 112, no. 17 (April 20, 2015): 5261–62. http://dx.doi.org/10.1073/pnas.1505313112.

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48

Van Berkel, Gary J., Gary L. Glish, Scott A. McLuckey, and Albert A. Tuinman. "High-pressure ammonia chemical ionization mass spectrometry and mass spectrometry/mass spectrometry for porphyrin structure determination." Energy & Fuels 4, no. 6 (November 1990): 720–29. http://dx.doi.org/10.1021/ef00024a018.

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49

Konstantinov, M. A., D. D. Zhdanov, and I. Yu Toropygin. "Quantitative mass spectrometry with <sup>18</sup>O labelling as an alternative approach for determining protease activity: an example of trypsin." Biological Products. Prevention, Diagnosis, Treatment 24, no. 1 (February 6, 2024): 46–60. http://dx.doi.org/10.30895/2221-996x-2024-24-1-46-60.

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SCIENTIFIC RELEVANCE. In the quality control of proteolytic enzyme components of medicinal products, the activity of proteases is determined by spectrophotometry, which involves measuring the amidase or esterase activity using a synthetic substrate and the proteolytic activity using the Anson method. These methods require special substrates and have low sensitivity; their specificity may be insufficient, which may lead to serious errors. Quantitative mass spectrometry is an alternative approach to protease activity assays, which involves adding an isotope-labelled peptide to hydrolysates of the test enzyme. This approach allows determining the activity of proteases, notably, by the hydrolysis of specific peptide bonds, while simultaneously confirming the identity and specificity of the test sample. Quantitative mass spectrometry has high sensitivity and does not require special substrates.AIM. This study aimed to investigate the possibility of enzymatic activity assay and enzyme identification by quantitative mass spectrometry with 18O labelling through an example of trypsin with casein.MATERIALS AND METHODS. The study used trypsin, casein, and H218O (Izotop, Russia). Peptide separation was performed using an Agilent 1100 HPLC system; mass spectra were obtained using a Bruker Ultraflex II MALDI-TOF/TOF mass spectrometer. Quantitative mass spectrometry was performed using a standard peptide, which was obtained from casein by tryptic digestion and HPLC purification. For 18O labelling, the authors dried the peptide and incubated it in H218О water. The quantitative analysis of the product was carried out using MALDI-TOF mass spectrometry. The authors used quantitative mass spectrometry with 18O labelling to determine enzymatic activity and calculate the Michaelis constant (KM).RESULTS. Following the tryptic digestion of casein, the authors identified the fragments corresponding to casein chains. The authors produced the isotope-labelled standard peptide and calculated its concentration using mass spectrometry. The authors determined the rate of casein digestion by trypsin and calculated the KM for trypsin, which was 13.65±0.60 μM. The standard deviation for repeated measurements showed that the mass-spectrometric method had a lower error of measurement than the spectrophotometric method. The sensitivity threshold for the mass-spectrometric method was 0.50±0.08 μM.CONCLUSIONS. The results obtained with trypsin confirm the possibility of enzymatic activity determination by the proposed method of quantitative mass spectrometry with 18O labelling. According to the sensitivity evaluation results, this method can be used for the simultaneous determination of enzyme activity, identity, and specificity. The proposed mass spectrometry approach is universal, it does not require expensive materials and reagents, and it can be easily adapted to determine the activity of virtually any protease.

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50

Sauvage, François-Ludovic, Franck Saint-marcoux, Bénédicte Duretz, Didier Deporte, Gérard Lachatre, and Pierre Marquet. "Screening of Drugs and Toxic Compounds with Liquid Chromatography-Linear Ion Trap Tandem Mass Spectrometry." Clinical Chemistry 52, no. 9 (September 1, 2006): 1735–42. http://dx.doi.org/10.1373/clinchem.2006.067116.

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Abstract Background: In clinical and forensic toxicology, general unknown screening is used to detect and identify exogenous compounds. In this study, we aimed to develop a comprehensive general unknown screening method based on liquid chromatography coupled with a hybrid triple-quadrupole linear ion trap mass spectrometer. Methods: After solid-phase extraction, separation was performed using gradient reversed-phase chromatography. The mass spectrometer was operated in the information-dependent acquisition mode, switching between a survey scan acquired in the Enhanced Mass Spectrometry mode with dynamic subtraction of background noise and a dependent scan obtained in the enhanced product ion scan mode. The complete cycle time was 1.36 s. A library of 1000 enhanced product ion–tandem mass spectrometry spectra in positive mode and 250 in negative mode, generated using 3 alternated collision tensions during each scan, was created by injecting pure solutions of drugs and toxic compounds. Results: Comparison with HPLC-diode array detection and gas chromatography-mass spectrometry for the analysis of 36 clinical samples showed that linear ion trap tandem mass spectrometry could identify most of the compounds (94% of the total). Some compounds were detected only by 1 of the other 2 techniques. Specific clinical cases highlighted the advantages and limitations of the method. Conclusion: A unique combination of new operating modes provided by hybrid triple-quadrupole linear ion trap mass spectrometers and new software features allowed development of a comprehensive and efficient method for the general unknown screening of drugs and toxic compounds in blood or urine.

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