Characterization of diamine oxidase from human seminal plasma

被引：6
|
作者：
Schwelberger, Hubert G. [1 ]
Feurle, Johannes [1 ]
Ahrens, Frank [2 ]
机构：
[1] Med Univ Innsbruck, Dept Visceral Transplant & Thorac Surg, Mol Biol Lab, A-6020 Innsbruck, Austria
[2] Univ Munich, Dept Vet Sci, Inst Anim Physiol, D-80539 Munich, Germany
来源：
JOURNAL OF NEURAL TRANSMISSION | 2013年 / 120卷 / 06期
基金：
奥地利科学基金会;
关键词：
Diamine oxidase; Copper amine oxidase; Histamine metabolism; Seminal plasma; Protein purification; PROTEINS;
D O I：
10.1007/s00702-013-0983-3
中图分类号：
R74 [神经病学与精神病学];
学科分类号：
摘要：
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.
引用
收藏
页码：983 / 986
页数：4
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