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Volume 58 (2010)
- Issue 6 Pages 195-
- Issue 5 Pages 167-
- Issue 4 Pages 123-
- Issue 3 Pages 93-
- Issue 2 Pages 35-
- Issue 1 Pages 1-
Volume 58, Issue 2
Displaying 1-5 of 5 articles from this issue
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INTEGRATED PAPER
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Shinsaku DOBASHI, Yoshiki YAMAGUCHI, Yoshinori IZAWA, Akihide WADA, Mi ...2010 Volume 58 Issue 2 Pages 35-46
Published: April 01, 2010
Released on J-STAGE: April 15, 2010
JOURNAL FREE ACCESSPersistent organic pollutants (POPs) are toxic chemicals that adversely affect human health and the environment around the world. The detection and evaluation of small amounts of POPs require methods with both high precision and high chemical selectivity. Conventional methods involve a number of preparatory steps and time-consuming analysis and are not suitable for the abovementioned purposes. Hence, new automated analysis methods are required for on-line detection and rapid analysis of POPs. In this paper, mass spectrometry with resonance-enhanced multi-photon ionization (REMPI) is performed to obtain information about the automated analysis of POPs in the gas-phase with on-line detection. Dynamic trapping time-of-flight mass spectrometry (TOFMS) was performed with sufficient selectivity and sensitivity for rapid analysis of polychlorinated biphenyls (PCBs) in the gas phase. Compared to normal trapping, the use of dynamic trapping enabled ion signal intensity to be increased by a factor of greater than 10. The detection limit at 1 min was <1 ppbV, and the accuracy also correlated well with the results of conventional analysis. Based on these results, an automated monitoring system was developed for automated analysis of PCBs. It was confirmed that this monitoring system was capable of analyzing PCB concentration without being influenced by main gas components or various coexisting substances, even under conditions characterized by exhaust gas and the work environment atmosphere. PCB concentration in PCB waste plants, which is substantially lower than the 0.10 mg/m3N specified in statutory regulations, could be analyzed within 1 min. It was possible to make continuous long-term analysis for over 2,000 h (120,000 points).View full abstractDownload PDF (1289K)
REVIEW
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—Ion Mobility Spectrometry—Toshiki SUGAI2010 Volume 58 Issue 2 Pages 47-73
Published: April 01, 2010
Released on J-STAGE: April 15, 2010
JOURNAL FREE ACCESSIon mobility spectrometry (IMS) has the same long history as mass spectrometry (MS). The method detects charged molecules not in vacuum but in buffer gas. Through the interaction between the charged molecules and the buffer gas, unique properties like structures, chiralities, and hydrophilicity of molecules can be observed by IMS. However, the resolution and the sensitivity of IMS are far less than those of MS limiting the applications of IMS. Those disadvantages have been resolved by the recent development of the ion and the vacuum handling techniques, which leads to hybrid spectrometry of IMS/MS (ion mobility spectrometry/mass spectrometry). Here we show the concept and recent progress on IMS, especially on IMS/MS, which have been opening new field in nano, bio, and environment sciences.View full abstractDownload PDF (3430K)
COMMENTARIES
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Kazumi SAIKUSA, Yo KONO, Shunsuke IZUMI2010 Volume 58 Issue 2 Pages 75-79
Published: April 01, 2010
Released on J-STAGE: April 15, 2010
JOURNAL FREE ACCESSWe investigated the topology and dynamics of melittin within the liposomes using mass spectrometry combined with acetylation. According to matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and matrix-assisted laser desorption/ionization quadrupole ion trap time-of-flight mass spectrometry/mass spectrometry (MALDI-QIT-TOF MS/MS) analyses, melittin within the liposomes was mono acetylated; with the acetylated position being the N-terminal of melittin. This acetylation followed first-order kinetics. The rate constant was less than that of the acetylation of melittin in aqueous solution. Thus, it is suggested that the observed rate constant is that for the release of the N-terminal region of melittin to a water phase from the hydrophobic core of the liposomes. This approach has opened a new method in the study of dynamics of transmembrane helices within the membranes using mass spectrometry.View full abstractDownload PDF (646K) -
Koshi IMAMI, Masaru TOMITA, Yasushi ISHIHAMA2010 Volume 58 Issue 2 Pages 81-87
Published: April 01, 2010
Released on J-STAGE: April 15, 2010
JOURNAL FREE ACCESSRecently, stable isotope labeling by amino acids in cell culture (SILAC) has become an essential technique for quantitative proteomics, enabling us to comprehensively compare the protein expression changes in different states of cells. However, several limitations have arisen from the conventional SILAC method with respect to the requirement of using dialyzed serum, quantification of unlabeled cells, and arginine-to-proline conversion. To overcome these limitations, we introduced a dual labeling SILAC approach, which does not require dialysis of serum. Here, we review the principle and the features of our SILAC method as well as its application to quantitative proteomics.View full abstractDownload PDF (1069K)
Letter to the Editor
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Shuichi SHIMMA2010 Volume 58 Issue 2 Pages 89-92
Published: April 01, 2010
Released on J-STAGE: April 15, 2010
JOURNAL FREE ACCESSDownload PDF (703K)
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