Journal of the Mass Spectrometry Society of Japan
Online ISSN : 1880-4225
Print ISSN : 1340-8097
ISSN-L : 1340-8097
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Volume 57, Issue 4
Displaying 1-11 of 11 articles from this issue
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REGULAR PAPER
  • An Application of Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry for Rapid Classification of Microorganism Isolated from Contact Lens Cases
    Taizo SUMIDE, Megumi TOYOHARA, Miya NOMACHI, Masahide TSUNODA, Kazuhik ...
    2009 Volume 57 Issue 4 Pages 241-248
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.241
    JOURNAL FREE ACCESS
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    As an alternative to commonly used biochemical, morphological, or gene technological analysis, we have evaluated a novel method for rapid classification of microorganism retrieved from used contact lens cases based on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS). Test microorganisms were isolated from contact lens cases. The cases were used daily for lens storage and care for 2 weeks. For this evaluation study, 659 microorganism isolates from the contact lens cases of 16 subjects were analyzed by MALDI-TOF-MS. The mass spectra obtained from the test isolates were compared with authentic spectra of a library database using application software Biotyper 2.0 (Bruker Daltonics). Results show that 644 of 659 (97.7%) isolates were successfully identified and classified into species by the MALDI-based method. Furthermore, these results were interpreted in terms of the risk of infectious disease. Our method is especially useful for simultaneous classification of a large number of test microorganisms because of fewer preparative steps and lower cost.
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NOTE
  • Quantitative Dynamic Analysis of Site-Specific Phosphorylation of Myelin Basic Protein Using Mass Spectrometry and iTRAQ Reagent
    Mamoru MATSUBARA, Fumihiko TSUCHIYA
    2009 Volume 57 Issue 4 Pages 249-254
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.249
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    Protein phosphorylation is a key post-translational modification that governs biological processes. Methods for monitoring the phosphorylation status of proteins are very important for the evaluation of diverse biological and pathological processes. Here we analyzed the site-specific phosphorylation of myelin basic protein (MBP) by protein kinase JNK1 (c-Jun N-terminal protein kinase) using liquid chromatography tandem mass spectrometry and iTRAQ reagent. Samples from time course reactions were differentially tagged using a multiplex reagent system, which enabled the simultaneous identification and relative quantification of phosphorylation. Three phosphorylation sites (Thr94, Thr97, and Ser164) were identified; all of them contained the JNK1 consensus sequence. The observed time course patterns can be classified into three different types corresponding to phosphorylated peptides, unphosphorylated peptides, and peptides with no phosphorylation sites. The method enables a better understanding of the complexities of kinase activity through the efficient analysis of time-dependent effects.
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INTEGRATED PAPER
COMMENTARIES
  • Application of 18O-Labeling Method to Structural Analysis of Chondroitin Sulfate Oligosaccharides
    Shigeyasu ITO
    2009 Volume 57 Issue 4 Pages 283-289
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.283
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    Numerous studies have been reported on structural analysis of chondroitin sulfate (CS) oligosaccharides using multiple-stage mass spectrometry (MSn). However, their sequence determination is highly complex because of the simply repeating backbone structure. This study attempts to overcome this issue using an 18O-labeling method. The usefulness of the 18O-labeling method in the MSn analysis of CS oligosaccharide is shown in this paper.
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  • Application of Liquid Chromatography Tandem Mass Spectrometry to Bioanalysis Services
    —Role of the “GLP (Good Laboratory Practice)-Free” Laboratory—
    Yasuko TSUKAZAKI, Hidehiko NAKANO, Naoto SENDA
    2009 Volume 57 Issue 4 Pages 291-300
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.291
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    Our GLP (Good Laboratory Practice)-free laboratory continues to develop state-of-the-art technologies that will provide a cutting-edge service to our clients.
    •We will respond to client requests promptly.
    •We will have a good relationship with clients from the early stage of new drug development. Our GLP-free laboratory can supply many technologies for application to GLP laboratories.
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  • Quantification of DNA Adducts by Using Liquid Chromatography/Tandem Mass Spectrometry
    Tomonari MATSUDA, Haruna NAGAYOSHI, Haruhiko SUGIMURA, Pei-Hsin CHOU
    2009 Volume 57 Issue 4 Pages 301-304
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.301
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    Formation of DNA adducts is a crucial step for carcinogenesis and aging. However, until recently, it was difficult to quantify trace amount of DNA adducts in living organisms. Development of liquid chromatography/tandem mass spectrometry (LC/MS/MS) equipments enables us to quantify DNA adducts at practical sensitivity. Molecular epidemiological study such as aldehyde dehydrogenase 2 gene (ALDH2) genotypes and risk of alcohol-related DNA damage has been conducted by using LC/MS/MS. Furthermore, we developed “DNA adductome” analysis which can display comprehensive picture of DNA adducts in living organisms. These techniques may contribute to understand mechanisms of carcinogenesis and aging.
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  • New Stacked Ring Ion Guide Design for Improving Ion Transmission
    Masayuki KUBOTA
    2009 Volume 57 Issue 4 Pages 305-307
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.305
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    We developed a new triple stage quadruple mass spectrometer equipped with a new ion guide based on “RF (radio frequency)-only stacked ring electrode technique.” This ion guide design improves ion transmission in differential pumping regions. This article introduces this design and its performance in comparison with traditional tube lens/skimmer lens designs.
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  • Charge-Number Discrimination Mass Analysis Using Superconducting Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometer
    —Analysis of Fragment Impurities in Immunoglobulin G—
    Kaori CHIBA, Masahiro UKIBE, Yiner CHEN, Shigetomo SHIKI, Masataka OHK ...
    2009 Volume 57 Issue 4 Pages 309-316
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.309
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    Conventional time-of-flight mass spectrometers equipped with microchannel plate (MCP) detectors give only m/z values, which remains ambiguous over charge number (z). In contrast, the matrix-assisted laser desorption/ionization (MALDI) TOF mass spectrometer (TOF-MS) with a superconducting tunnel junction (STJ) detector—Super-TOF-MS—enables kinetic energy measurement with mass-independent detection efficiency. Therefore, since kinetic energy is proportional to z, it is possible to determine mass (m) unambiguously.
    The Super-TOF-MS is effective for analysing high-mass fragments in immunoglobulin solution. Specifically, unknown peaks appearing on mass spectra for immunoglobulin G (IgG) samples can be identified as IgG fragments using kinetic energy measurements and the mass-independent detection efficiency of the STJ detector. A complete IgG molecule has two heavy and two light chains that are connected by disulfide bonds. The heavy and light chains include four and two structural domains, respectively (12 domains in total). The charge-state discrimination mass analysis enables the assignment of m values to the unknown peaks. The existence of pairs for which the m-value sum is equal to that of the intact IgG reveals that there are several fragment types consisting of different numbers of structural domain units.
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  • Utility of Application of Liquid Chromatography/Triple Stage Mass Spectrometry (LC/MS3) for Proteome Analysis
    Kiyonaga FUJII, Tomoyo NAKANO, Fumihiko USUI, Yasuhiko BANDO, Fuyuhiko ...
    2009 Volume 57 Issue 4 Pages 317-325
    Published: August 01, 2009
    Released on J-STAGE: August 15, 2009
    DOIhttps://doi.org/10.5702/massspec.57.317
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    Protein identification via mass spectrometry (MS) relies primarily on protein sequence databases. Identification resulting from a sequence database search in the tandem mass spectrometry (MS/MS) experiments for the digested peptides is derived from an algorithm based on statistical confidence, and therefore, it often pro- ides false-positive identifications. Although one can apply high-resolution MS such as Fourier-transform mass spectrometer (FT-MS) to obtain results with high confidence, the instrumentation is expensive and the results are still probability based. Therefore, we introduced data-dependent triple stage mass spectrometry (MS3) into our well-established liquid chromatography/tandem mass spectrometry (LC/MS/MS) analysis of linear ion trap MS to achieve evidence-based protein identification. Peptide sequencing by MS3 analysis can provide a direct evidence for a sequence elucidated by MS/MS data and help determine whether the search results are correct.
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Letter to the Editor
Message from the President
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