Heparin-binding motif mutations of human diamine oxidase allow the development of a first-in-class histamine-degrading biopharmaceutical

eLife

Kornelia Schuetzenberger¹  Karin Petroczi²  Marlene Resch³  Elisabeth Gludovacz⁴  Jürgen Pollheimer⁴  Sigrid Vondra⁴  Thomas Boehm⁴  Markus Schosserer⁵  Katharina Tillmann⁵  Nicole Borth⁵  Tiina A Salminen⁶  Serhii Vakal⁶  Gerald Klanert⁷  Bernd Jilma⁷ 

[1] Department of Clinical Pharmacology, Medical University of Vienna, Vienna, Austria;Center for Biomedical Research, Medical University of Vienna, Vienna, Austria;Center for Medical Physics and Biomedical Engineering, Medical University of Vienna, Vienna, Austria;Department of Biotechnology, University of Natural Resources and Life Sciences, Vienna, Austria;Department of Clinical Pharmacology, Medical University of Vienna, Vienna, Austria;Department of Obstetrics and Gynecology, Medical University of Vienna, Vienna, Austria;Strutural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland;

关键词: diamine oxidase;    histamine;    heparin;    heparan sulfate proteoglycan;    clearance;    half-life;   

DOI  :  10.7554/eLife.68542

来源: DOAJ

【 授权许可】

Unknown