Related Experiment Video
Updated: May 14, 2026
The Examination of Peroxidase-Positive Leukocytes in Semen
Published on: January 19, 2024
Characterization of diamine oxidase from human seminal plasma
Hubert G Schwelberger1, Johannes Feurle, Frank Ahrens
1Molecular Biology Laboratory, Department of Visceral, Transplant and Thoracic Surgery, Medical University Innsbruck, Schöpfstrasse 41, 6020, Innsbruck, Austria. hubert.schwelberger@i-med.ac.at
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.
