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Characterization of diamine oxidase from human seminal plasma

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Abstract

Diamine oxidase (DAO) was purified to homogeneity from human seminal plasma by consecutive chromatographic fractionation on heparin-sepharose, phenyl-sepharose, CIM-QA, and Superdex 200. Human seminal plasma DAO behaves electrophoretically similar to DAO proteins from other human tissues and has very similar enzymatic properties with histamine and aliphatic diamines being the preferred substrates as well as significant conversion of polyamines. The cellular source and functional importance of DAO in human semen remain to be determined.

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Acknowledgments

This work was supported by grants from the Austrian Science Fund and by COST Action BM0806.

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  The authors declare that they have no conflict of interest.

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Authors and Affiliations

  1. Molecular Biology Laboratory, Department of Visceral, Transplant and Thoracic Surgery, Medical University Innsbruck, Schöpfstraße 41, 6020, Innsbruck, Austria

    Hubert G. Schwelberger & Johannes Feurle

  2. Department of Veterinary Sciences, Institute of Animal Physiology, Ludwig-Maximilians University Munich, Veterinärstraße 13, 80539, Munich, Germany

    Frank Ahrens

Authors
  1. Hubert G. Schwelberger
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  2. Johannes Feurle
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  3. Frank Ahrens
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Correspondence to Hubert G. Schwelberger.

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Schwelberger, H.G., Feurle, J. & Ahrens, F. Characterization of diamine oxidase from human seminal plasma. J Neural Transm 120, 983–986 (2013). https://doi.org/10.1007/s00702-013-0983-3

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  • DOI: https://doi.org/10.1007/s00702-013-0983-3

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