Journal of the Mass Spectrometry Society of Japan
Online ISSN : 1880-4225
Print ISSN : 1340-8097
ISSN-L : 1340-8097
54 巻, 5 号
選択された号の論文の16件中1~16を表示しています
技術報告
  • Atsushi TAKAMIZAWA, Mayo SHIMOKAWA, Hiroaki MAEDA, Hideki YAMADA, Yuta ...
    2006 年 54 巻 5 号 p. 183-186
    発行日: 2006年
    公開日: 2006/10/03
    ジャーナル フリー
    New liquid chromatography/mass spectrometry (LC/MS) coupled with a new interface, LC/laser spray MS was developed. The laser spray was found to be particularly suitable for the low-concentration aqueous sample solutions because the enrichment of the sample concentration takes place near the meniscus of the liquid sample protruded from the stainless steel capillary. The extracts from the young leaves were measured using the present method coupled with the dual spray technique. Owing to much better sensitivities for laser spray than for electrospray, molecular formulas for some components in the sample could be postulated.
  • Seketsu FUKUZAWA, Miwako ASANUMA, Kazuo TACHIBANA, Hiroshi HIROTA
    2006 年 54 巻 5 号 p. 187-193
    発行日: 2006年
    公開日: 2006/10/03
    ジャーナル フリー
    A new screening method to detect protein-ligand interactions has been developed through a combination of mixed self-assembled monolayer (SAM) and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). The mixed SAM surface was prepared on flat gold plate from a mixture of 20-mercapto-3,6,9-trioxaicosanol and a ligand-bound derivative of 29-mercapto-3,6,9,12,15,18-hexaoxanonacosanol. This surface is very suitable for observing the molecular interaction accurately, because there is very low levels of steric hindrance between immobilized ligands and the non-charged hydroxyl groups of polyethylene glycol which resists from the non-specific adsorption of biomolecules. Because the surface coated with the mixed SAM is washable with water, it can be used directly as a probe for MALDI-MS, a technique commonly used for the annotation of protein function. As an example we report here the selective detection of the molecular interaction between a Src homology 3 (SH3) domain of human p85α phosphatidylinositol 3-kinase (PI3K) and its ligand peptide (H-RKLPPRPAF-OH) attached covalently to mixed SAM using MALDI-MS.
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