Characterization of diamine oxidase from human seminal plasma.
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.
Molecular Biology Laboratory, Department of Visceral, Transplant and Thoracic Surgery, Medical University Innsbruck, Schöpfstrasse 41, 6020, Innsbruck, Austria. hubert.schwelberger@i-med.ac.at
Hubert G
HG
Schwelberger
Johannes
J
Feurle
Frank
F
Ahrens
D000328:Adult; D006631:Amine Oxidase (Copper-Containing) / Q000378:metabolism*; D006801:Humans; D008297:Male; D008875:Middle Aged; D011073:Polyamines; D012661:Semen / Q000201:enzymology*; D012685:Sepharose / Q000031:analogs & derivatives
D011073:Polyamines; C020927:phenyl-sepharose; D012685:Sepharose; D006631:Amine Oxidase (Copper-Containing)