Expression of human beta-N-acetylhexosaminidase B in yeast eases the search for selective inhibitors

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F16%3A00461990" target="_blank" >RIV/61388971:_____/16:00461990 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.enzmictec.2016.03.003" target="_blank" >http://dx.doi.org/10.1016/j.enzmictec.2016.03.003</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.enzmictec.2016.03.003" target="_blank" >10.1016/j.enzmictec.2016.03.003</a>

Result language
angličtina
Original language name
Expression of human beta-N-acetylhexosaminidase B in yeast eases the search for selective inhibitors
Original language description
Human lysosomal beta-N-acetylhexosaminidases from the family 20 of glycoside hydrolases are dimeric enzymes catalysing the cleavage of terminal beta-N-acetylglucosamine and beta-N-acetylgalactosamine residues from a broad spectrum of glycoconjugates. Here, we present a facile, robust, and cost-effective extracellular expression of human beta-N-acetylhexosaminidase B in Pichia pastoris KM71H strain. The prepared Hex B was purified in a single step with 33% yield obtaining 10 mg of the pure enzyme per 1 L of the culture media.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Project
<a href="/en/project/GC15-02578J" target="_blank" >GC15-02578J: Modified multivalent poly-N-acetyllactosamine glycans as novel ligands of human galectin-3</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2016
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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