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High-Sensitivity Mass Spectrometry for Analysis of Posttranslational Modifications

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Abstract

Pulsed fast atom bombardment ionization (pulsed-FAB) mass spectrometry has been developed to improve the sensitivity of tandem mass spectrometry (MS/MS), allowing it to be used for the analysis of very small samples. MS/MS, when used with a magnetic four-sector instrument coupled with the pulsed-FAB system, allows significant enhancement in product ion intensity of over ten-fold in magnitude over conventional FAB. MS/MS was applied to the structural analysis of a unique nuclear protein, designated p28, which was isolated from a histone fraction obtained from starfish testes. The results clearly show that protein p28 is a heterodimer composed of testicular histones H2B and H4 which are cross-linked between Gln9 of H2B and Lys5 of H4.

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Authors and Affiliations

  1. Institute for Protein Research, Osaka University, Yamadaoka 3-2, Suita, Osaka, 565, Japan

    Toshifumi Takao & Yasutsugu Shimonishi

  2. Department of Applied Biochemistry, Hiroshima University, Kagamiyama 1-4-4, Higashi-hiroshima, Hiroshima, 739, Japan

    Takahiko Shimizu & Susumu Ikegami

Authors
  1. Toshifumi Takao
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  2. Takahiko Shimizu
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  3. Susumu Ikegami
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  4. Yasutsugu Shimonishi
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Takao, T., Shimizu, T., Ikegami, S. et al. High-Sensitivity Mass Spectrometry for Analysis of Posttranslational Modifications. J Protein Chem 16, 409–413 (1997). https://doi.org/10.1023/A:1026388806194

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  • DOI: https://doi.org/10.1023/A:1026388806194

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