Journal of the Mass Spectrometry Society of Japan
Online ISSN : 1880-4225
Print ISSN : 1340-8097
ISSN-L : 1340-8097
55 巻, 1 号
選択された号の論文の9件中1~9を表示しています
一般論文
  • Toshikazu MINAMISAWA, Kiyoshi SUZUKI, Hiroshi MAEDA, Satoshi SHIMOKATA ...
    2007 年 55 巻 1 号 p. 1-6
    発行日: 2007年
    公開日: 2007/02/15
    ジャーナル フリー
    Both saturated and unsaturated forms of isomeric unsulfated glycosaminoglycan (GAG) oligosaccharides, i.e., tetrasaccharides of chondroitin (CH) and hyaluronan (HA), were analyzed by electrospray ionization mass spectrometry/mass spectrometry. Although the only structural difference between them was the hydroxyl group at the C-4 position in N-acetylhexosamine (GalNAc or GlcNAc, respectively), given the same m/z value of precursor ions, these isomers in both their saturated and unsaturated forms could be separated by careful examination of diagnostic fragment ions in their product ion mass spectra when the relative abundances of these fragment ions were considered. In addition, the product ion mass spectrum of the unsaturated HA tetrasaccharide was compared with its linkage isomer, N-acetylheparosan tetrasaccharide. In this case, the isomers were more easily differentiated by comparing their characteristic spectral patterns. By adopting this approach, systematic differentiation of isomeric unsulfated GAG oligosaccharides should be achieved by means of fragmentation. It should also contribute widely to GAG-related biochemical and medicinal research in the future.
  • Akio HAYASHI, Noriko TANIGUCHI, Kazuo TSUJIMOTO, Isao KUBO
    2007 年 55 巻 1 号 p. 7-13
    発行日: 2007年
    公開日: 2007/02/15
    ジャーナル フリー
    Formation of ε complex with 2-hydroxy-6-[8′(Z),11′(Z),14′-pentadecatrienyl]benzoic acid (anacardic acid) and copper ion in the respective ratios of 2 : 1 and 1 : 1 at room temperature was observed by electrospray ionization mass spectrometry. The oxidation of 3-(3,4-dihydroxyphenyl)alanine (DOPA) in the presence of anacardic acid showed competitive inhibition with temporary reduction from dopaquinone to DOPA. In the oxidation of neurotensin, the oxidized products, dopaquinone-derivatives, were observed. Mass spectrometry revealed that the enzymatic oxidation of tyrosine residue is inhibited by anacardic acid.
  • 豊田 岐聡, 西口 克
    2007 年 55 巻 1 号 p. 17-24
    発行日: 2007年
    公開日: 2007/02/15
    ジャーナル フリー
    The ion beam profiles of the multi-turn time-of-flight mass spectrometers “MULTUM” and “MULTUM II” were simulated using the ion trajectory simulation program “TRIO 2.0.” These ion optical systems satisfy the “perfect focusing” conditions and are suitable for an imaging mass spectrometer in stigmatic mode. From the simulation, it was clear that the higher order aberration of MULTUM II is smaller than that of MULTUM. A smaller initial lateral angular deviation makes aberration after circulation smaller in both the ion optical systems. In the ion optical system MULTUM II, the ion images should be measured at even numbered cycles, because the second-order coefficient (x¦xx) will be cancelled after every two cycles.
  • 杉浦 悠毅, 新間 秀一, 森山 泰亘, 瀬藤 光利
    2007 年 55 巻 1 号 p. 25-31
    発行日: 2007年
    公開日: 2007/02/15
    ジャーナル フリー
    Direct tissue analysis and ion imaging using mass spectrometry extract significant information directly from complex biological samples. In this paper, we introduce a method for the direct analysis of cultured cells. To analyze cultured cells by direct mass spectrometry (MS), we incubated HEK293T cells directly on an indium-tin-oxide layer on polyethylene terephthalate film. After fixation of cells on the film, matrix application was performed by spray-droplet method, which is a two-step matrix application method to improve the ionization efficiency of biological tissue samples. By direct MS of HEK293T cells, we obtained mass spectra of approximately 350 protein signals with good quality. Furthermore, we profiled proteins as digested products and identified major signals by applying an on-tissue digestion direct MS/MS method, which is the procedure for enzymatic protein digestion of biological tissue samples. This new approach enables proteomic analysis directly from the cell culture system.
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