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Journal of Neural Transmission

, Volume 120, Issue 6, pp 983–986 | Cite as

Characterization of diamine oxidase from human seminal plasma

  • Hubert G. SchwelbergerEmail author
  • Johannes Feurle
  • Frank Ahrens
Translational Neurosciences - Short communication

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.

Keywords

Diamine oxidase Copper amine oxidase Histamine metabolism Seminal plasma Protein purification 

Notes

Acknowledgments

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

Conflict of interest

  The authors declare that they have no conflict of interest.

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Copyright information

© Springer-Verlag Wien 2013

Authors and Affiliations

  • Hubert G. Schwelberger
    • 1
    Email author
  • Johannes Feurle
    • 1
  • Frank Ahrens
    • 2
  1. 1.Molecular Biology Laboratory, Department of Visceral, Transplant and Thoracic SurgeryMedical University InnsbruckInnsbruckAustria
  2. 2.Department of Veterinary SciencesInstitute of Animal Physiology, Ludwig-Maximilians University MunichMunichGermany

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