Show simple item record

dc.contributor.authorWinkler, S
dc.contributor.authorSchweiger, D
dc.contributor.authorWei, Zheng
dc.contributor.authorRajkovic, E
dc.contributor.authorKungl, A
dc.date.accessioned2014-04-17T14:38:03Z
dc.date.available2014-04-17T14:38:03Z
dc.date.issued2014-01-14
dc.identifier.citationBacterial expression and functional reconstitution of human heparanase. 2014: Carbohydr Resen
dc.identifier.issn1873-426X
dc.identifier.pmid24656445
dc.identifier.doi10.1016/j.carres.2014.01.002
dc.identifier.urihttp://hdl.handle.net/10541/315924
dc.description.abstractHuman heparanase is a heparan sulfate degrading enzyme located in the extracellular matrix playing a decisive role in angiogenesis and tumor metastasis. Translated as a 65kDa inactive prae-form, the protein is processed into an 8kDa and a 50kDa subunit which form a non-covalently associated active heterodimer. We have expressed the two subunits separately in Escherichia coli which yielded active human heparanase upon reconstitution. The two purified subunits folded independently and secondary structure analysis by far-UV CD spectroscopy gave 33.1/11.1% α/β content for the 50kDa subunit and 6.9/49% α/β content for the 8kDa subunit. This heparanase expression system is easy and can be used for efficient screening for enzyme inhibitors.
dc.languageENG
dc.language.isoenen
dc.rightsArchived with thanks to Carbohydrate researchen
dc.titleBacterial expression and functional reconstitution of human heparanase.en
dc.typeArticleen
dc.contributor.departmentDepartment of Pharmaceutical Sciences, University of Graz, Humboldtstrasse 46, 8010 Graz, Austriaen
dc.identifier.journalCarbohydrate Researchen
html.description.abstractHuman heparanase is a heparan sulfate degrading enzyme located in the extracellular matrix playing a decisive role in angiogenesis and tumor metastasis. Translated as a 65kDa inactive prae-form, the protein is processed into an 8kDa and a 50kDa subunit which form a non-covalently associated active heterodimer. We have expressed the two subunits separately in Escherichia coli which yielded active human heparanase upon reconstitution. The two purified subunits folded independently and secondary structure analysis by far-UV CD spectroscopy gave 33.1/11.1% α/β content for the 50kDa subunit and 6.9/49% α/β content for the 8kDa subunit. This heparanase expression system is easy and can be used for efficient screening for enzyme inhibitors.


Files in this item

This item appears in the following Collection(s)

Show simple item record