<div class="csl-bib-body">
<div class="csl-entry">Bonifert, G. (2015). <i>Glyco-engineered horseradish peroxidase for targeted cancer treatment</i> [Diploma Thesis, Technische Universität Wien]. reposiTUm. https://doi.org/10.34726/hss.2015.26245</div>
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dc.identifier.uri
https://doi.org/10.34726/hss.2015.26245
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dc.identifier.uri
http://hdl.handle.net/20.500.12708/9037
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dc.description
Abweichender Titel laut Übersetzung der Verfasserin/des Verfassers
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dc.description
Zsfassung in dt. Sprache
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dc.description.abstract
The oxidoreductase horseradish peroxidase (HRP; EC 1.11.1.7) reacts with the plant hormone indole-3-acetic acid (IAA) to a cytotoxin and induces cell apoptosis. This feature can be used for targeted cancer therapy by transporting both the enzyme and the hormone to the cancer cells by antibody conjugation. Recombinant HRP, produced in the yeast Pichia pastoris, carries hypermannosylation on the enzyme surface. Due to this fact, the recombinant enzymes are not qualified for medical applications as there can be problems with antibody conjugation due to hyperglycosylation and furthermore these non-native extensive glycan chains can lead to immunogenic reactions in the patients. In this Thesis, 5 novel recombinant HRP variants were generated with reduced surface glycosylation. Two HRP variants described the isoenzyme HRP C1A but were expressed in glyco-engineered Pichia pastoris strains, whereas the other 3 variants described a mutated enzyme expressed as well in glyco-engineered Pichia pastoris strains. The enzyme with the most promising characteristics in terms of catalytic activity and stability was produced in the controlled environment of a bioreactor in batch and fed-batch mode. The purified and biochemically characterized enzymes (HRP with reduced glycosylation pattern, plant-HRP and wildtype-HRP for reference) were tested for their interactions and effects on cancer cell lines with IAA. The cytotoxicity studies revealed that the recombinant enzymes are a powerful tool and promising candidate for cancer treatment.
en
dc.language
English
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dc.language.iso
en
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dc.rights.uri
http://rightsstatements.org/vocab/InC/1.0/
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dc.subject
HRP
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dc.subject
peroxidase
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dc.subject
glycosylation
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dc.subject
glyco-engineering
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dc.subject
Pichia pastoris
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dc.subject
cancer treatment
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dc.title
Glyco-engineered horseradish peroxidase for targeted cancer treatment
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dc.title.alternative
Glyco-modifizierte Kren Peroxidase für gezielte Krebsbekämpfung
de
dc.type
Thesis
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dc.type
Hochschulschrift
de
dc.rights.license
In Copyright
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dc.rights.license
Urheberrechtsschutz
de
dc.identifier.doi
10.34726/hss.2015.26245
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dc.contributor.affiliation
TU Wien, Österreich
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dc.rights.holder
Günther Bonifert
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tuw.version
vor
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tuw.thesisinformation
Technische Universität Wien
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dc.contributor.assistant
Spadiut, Oliver
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tuw.publication.orgunit
E166 - Inst. f. Verfahrenstechnik, Umwelttechnik und Techn. Biowissenschaften