Zobrazeno 1 - 7 of 7 pro vyhledávání: '"thermolysine"'
1
Dissertation/ Thesis
Développement d'un nouveau biocapteur enzymatique ultrasensible pour la détection conductimétrique de l'ochratoxine A dans l'huile d'olive
Autor: Dridi, Fatma
Dans ce travail, nous nous sommes intéressés au développement d’un nouveau biocapteur enzymatique ultrasensible pour la détection conductimétrique d’une mycotoxine, l’ochratoxine A (OTA). Une peptidase, la thermolysine (TLN), a été chois
Externí odkaz: http://www.theses.fr/2016LYSE1018/document
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2
Development of a new ultra sensitive enzymatic biosensor for ochratoxin : a conductometric detection in olive oil
Autor: Dridi, Fatma
Publikováno v: Ingénierie des aliments. Université de Lyon, 2016. Français. ⟨NNT : 2016LYSE1018⟩
A new ultrasensitive enzymatic biosensor for the direct conductometric detection of ochratoxin A (OTA) has been developed in this work. Thermolysin (TLN), a peptidase, was chosen as recognition element. The proposed biosensor is based on TLN immobili
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::759174ff5e03b72bfb5c883a23b605d4
https://theses.hal.science/tel-01362941
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3
The selective biotin tagging and thermolysin proteolysis of chloroplast outer envelope proteins reveals information on protein topology and association into complexes
Autor: Hélène eHardré, Lauriane eKuhn, Catherine eAlbrieux, Juliette eJouhet, Morgane eMichaud, Daphné eSeigneurin-Berny, Denis eFalconet, Maryse A. Block, Eric eMarechal
Publikováno v: Frontiers in Plant Science
Frontiers in Plant Science, Frontiers, 2014, 5, pp.1-15. ⟨10.3389/fpls.2014.00203⟩
Frontiers in Plant Science (5), 1-15. (2014)
Frontiers in Plant Science, Vol 5 (2014)
Frontiers in Plant Science, Frontiers, 2014, 5 (3), pp.203
Frontiers in Plant Science, 2014, 5, pp.1-15. ⟨10.3389/fpls.2014.00203⟩
International audience; The understanding of chloroplast function requires the precise localization of proteins in each of its sub-compartments. High-sensitivity mass spectrometry has allowed the inventory of proteins in thylakoid, stroma, and envelo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::037679f6bf2e281ea1c4ae6bedb17798
https://hal.inrae.fr/hal-02637436
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4
The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro
Autor: Ann Beaumont, Michael J. O’Donohue
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1996, 271 (43), pp.26477-26481. ⟨10.1074/jbc.271.43.26477⟩
Journal of Biological Chemistry, 1996, 271 (43), pp.26477-26481. ⟨10.1074/jbc.271.43.26477⟩
ResearcherID
Journal of Biological Chemistry 43 (271), 26477-26481. (1996)
Next Section Abstract The zinc endopeptidase thermolysin (EC 3.4.24.27), an extracellular enzyme from Bacillus thermoproteolyticus, is synthesized as a preproprotein, with the prosequence (204 residues) being two-thirds the size of the mature enzyme
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7720845584666bb61c93448bea0d75d8
https://pubmed.ncbi.nlm.nih.gov/8900115
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7
The role of histidine 231 in thermolysin-like enzymes
Autor: Marie-Claude Fournie-Zaluski, Bernard P. Roques, M. Assicot, Nathalie Rousselet, Claude Bohuon, Michael J. O’Donohue, Nathalie Paredes, Ann Beaumont
Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1995, 270 (28), pp.16803-16808. ⟨10.1074/jbc.270.28.16803⟩
Journal of Biological Chemistry, 1995, 270 (28), pp.16803-16808. ⟨10.1074/jbc.270.28.16803⟩
Journal of Biological Chemistry 28 (270), 16803-16808. (1995)
In the zinc metallopeptidases produced by the genus Bacillus, an active site histidine has been proposed to either stabilize the transition state in catalysis by donating a hydrogen bond to the hydrated peptide (Matthews, B. W.(1988) Acc. Chem. Res.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f8f6ed7ff851940e0996f71dc63895a
https://hal.inrae.fr/hal-02711870/document
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