Journal of the Mass Spectrometry Society of Japan
Online ISSN : 1880-4225
Print ISSN : 1340-8097
ISSN-L : 1340-8097
63 巻, 4 号
選択された号の論文の3件中1~3を表示しています
一般論文
  • 横山 祐介, 岡 秀行
    2015 年 63 巻 4 号 p. 83-92
    発行日: 2015/08/01
    公開日: 2015/08/15
    ジャーナル フリー
    Chitooligosaccharides are used in medicines, cosmetics and foods due to their bioactivity and non-toxicity in the human body. Because they are frequently present as complex mixtures, with various degrees of polymerization, degrees of acetylation and isobars that have a number of sequences, simultaneous analysis can be a challenging task. Here, we report on a method for the simultaneous sequencing of chitooligosaccharides by the UHPLC-tandem MS analysis. Chitooligosaccharides that were produced by digestion with chitinase were labeled with 2-aminopyridine to label the reducing end. After the purification by preparative-SEC, we identified the sequence of chitooligosaccharides (DP 1–5) from MS/MS spectra by the UHPLC-tandemMS analysis. In this method, the MSn analysis, the decrease in the sensitivity of MS spectra is not important, because the chitooligosaccharides are first separated by chromatography. This sequencing method can be used in the characterization of deacetylase and structural studies of other bioactive chitooligosaccharides.
総合論文
  • —酸化タンパク質への応用—
    絹見 朋也
    2015 年 63 巻 4 号 p. 93-99
    発行日: 2015/08/01
    公開日: 2015/08/15
    ジャーナル フリー
    Proteins can be modified at the peptide backbone and the amino acid side chains, the process is so called post-translational modification. The modifications are divided into two classes of modification reaction, enzymatic reaction and non-enzymatic reaction. The typical examples of non-enzymatic modification are carbonylation, oxidation in methionine and cysteine, deamidation in aspartate and glutamate, glycation in N-terminal and amino group of lysine. Most of these modifications are irreversible and known to be implicated in cellular damage, ageing and disease. Mass spectrometry has been extensively contributing to this field of the structural characterization and quantitation. In this paper, I present identification and structural determination of oxidatively modified protein and the application to biomarker discovery, and also described the technical considerations to deal with these non-enzymatic modifications from the point of view of mass spectrometry. One of the topics is the structure determination of carbonylated protein from complex mixture obtained by the use of isotopically labeled hydrazine compound with matrix-assisted laser desorption ionization mass spectrometry. The potential protein biomarker for Parkinson's disease found by mass spectrometry is also discussed.
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