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- Original title:
- Rekombinante Expression, Rückfaltung und biochemische Charakterisierung verschiedener Formen der Kallikrein-ähnlichen Protease 15 (KLK15)
- Translated title:
- Recombinant expression, refolding and biochemical characterization of various forms of kallikrein-related peptidase 15 (KLK15)
- Author:
- Schwarz, Michaela Amélie
- Year:
- 2014
- Document type:
- Dissertation
- Faculty/School:
- Fakultät für Medizin
- Advisor:
- Magdolen, Viktor (Prof. Dr.)
- Referee:
- Magdolen, Viktor (Prof. Dr.); Schmitt, Manfred (Prof. Dr.)
- Language:
- de
- Subject group:
- MED Medizin
- Keywords:
- Kallikrein-ähnliche Protease KLK15, Spleißvariante KLK15ntfl, rekombinante Expression, Rückfaltung, fluorogene Substrattests, Trypsin-ähnliche Aktivität, limitierte Proteolyse
- Translated keywords:
- human Kallikrein-related peptidase 15 (KLK15), splice variant KLK15ntfl, protein refolding, fluorogenic substrate testing, trypsin-like activity, limited proteolysis
- Abstract:
- In der vorliegenden Arbeit wurden verschiedene Formen der Kallikrein-ähnlichen Protease 15 (KLK15) und ihrer Spleißvariante KLK15ntfl in E.coli produziert, gereinigt und rückgefaltet. Fluorogene Substrattests zeigten für mature KLK15, nicht aber für KLK15ntfl, eine Trypsin-ähnliche Aktivität. Die Produktion des "natürlichen" pro-Enzyms von KLK15/KLK15ntfl erlaubte zudem die Analyse potentieller KLK15-Aktivatoren. Die untersuchten KLK-Proteasen (KLK4-8, 10, 11) waren jedoch nicht in der Lage KLK1... »
- Translated abstract:
- In the present work, various forms of human kallikrein-related peptidase 15 (KLK15) and its splice variant KLK15ntfl were produced in E.coli, purified and refolded. Fluorogenic substrate testings revealed a trypsin-like activity for mature KLK15, KLK15ntfl displayed no detectable activity. Furthermore, the production of the "natural" pro-enzyme of KLK15/KLK15ntfl allowed the analysis of potential KLK15-activators. The tested KLK-proteases (KLK4-8, 10, 11) however were not able to activate KLK15... »
- Series:
- Biological chemistry
- WWW:
- https://mediatum.ub.tum.de/?id=1141615
- Date of submission:
- 23.04.2013
- Oral examination:
- 08.05.2014
- File size:
- 3430018 bytes
- Pages:
- 132
- Urn (citeable URL):
- https://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:91-diss-20140508-1141615-0-4
- Last change:
- 21.05.2014
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