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    Bacterial expression and functional reconstitution of human heparanase.

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    Authors
    Winkler, S
    Schweiger, D
    Wei, Zheng
    Rajkovic, E
    Kungl, A
    Affiliation
    Department of Pharmaceutical Sciences, University of Graz, Humboldtstrasse 46, 8010 Graz, Austria
    Issue Date
    2014-01-14
    
    Metadata
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    Abstract
    Human 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.
    Citation
    Bacterial expression and functional reconstitution of human heparanase. 2014: Carbohydr Res
    Journal
    Carbohydrate Research
    URI
    http://hdl.handle.net/10541/315924
    DOI
    10.1016/j.carres.2014.01.002
    PubMed ID
    24656445
    Type
    Article
    Language
    en
    ISSN
    1873-426X
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.carres.2014.01.002
    Scopus Count
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    All Paterson Institute for Cancer Research

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