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01-06-2013 | Translational Neurosciences - Short communication

Characterization of diamine oxidase from human seminal plasma

Authors: Hubert G. Schwelberger, Johannes Feurle, Frank Ahrens

Published in: Journal of Neural Transmission | Issue 6/2013

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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Title: Characterization of diamine oxidase from human seminal plasma
Authors: Hubert G. Schwelberger
Johannes Feurle
Frank Ahrens
Publication date: 01-06-2013
Publisher: Springer Vienna
Published in: Journal of Neural Transmission / Issue 6/2013
Print ISSN: 0300-9564
Electronic ISSN: 1435-1463
DOI: https://doi.org/10.1007/s00702-013-0983-3

At a glance: The STEP trials

Springer Medicine

Characterization of diamine oxidase from human seminal plasma

Abstract

At a glance: The STEP trials

Springer Medicine

Abstract

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