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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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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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