Journal of the Mass Spectrometry Society of Japan
Online ISSN : 1880-4225
Print ISSN : 1340-8097
ISSN-L : 1340-8097
57 巻, 4 号
選択された号の論文の11件中1~11を表示しています
一般論文
  • 角出 泰造, 豊原 恵, 野町 美弥, 角田 真英, 中田 和彦, 石田 康行
    2009 年 57 巻 4 号 p. 241-248
    発行日: 2009/08/01
    公開日: 2009/08/15
    ジャーナル フリー
    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.
ノート
  • 松原 守, 土屋 文彦
    2009 年 57 巻 4 号 p. 249-254
    発行日: 2009/08/01
    公開日: 2009/08/15
    ジャーナル フリー
    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.
総合論文
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Letter to the Editor
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