Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Caroline Vignaud"'
Publikováno v:
Biochimica et biophysica acta. 1864(9)
A controversy exists with respect to the mechanism of l-2-hydroxy acid oxidation by members of a family of FMN-dependent enzymes. A so-called carbanion mechanism was initially proposed, in which the active site histidine abstracts the substrate α-hy
Publikováno v:
Journal of Chromatography A. 1031:125-133
Methods for quantification of oxidised and reduced forms of glutathione (GSSG and GSH) and cysteine (CSSC and CSH) and the disulphide glutathione–cysteine (GSSC) resulting from the oxidation of the mixture of CSH and GSH are performed by RP-HPLC wi
Publikováno v:
Journal of Food Science. 67:2016-2022
Sulfhydryl oxidase (SOX) was purified after extraction and the contaminating catalase activity was completely eliminated in the last chromatography step. A yield of 25% was obtained with a purification factor higher than 300. The isoelectric point wa
Publikováno v:
Journal of Agricultural and Food Chemistry. 48:1050-1057
Two isoforms of catalase, CAT-1 and CAT-2, were purified from wheat germ after extraction, ammonium sulfate precipitations, hydrophobic chromatography, and two ionic-exchange chromatographies. The global yields and the purification factors were close
Autor:
Françoise Guéritte, Zhi-wei Chen, Daniel Guenard, Adil Jaafar, Florence Lederer, Caroline Vignaud, F. Scott Mathews, Bernard I. Levy
Publikováno v:
Biochimie
Biochimie, Elsevier, 2012, 94 (5), pp.1172-9. ⟨10.1016/j.biochi.2012.02.003⟩
Biochimie, Elsevier, 2012, 94 (5), pp.1172-9. ⟨10.1016/j.biochi.2012.02.003⟩
International audience; Long chain hydroxy acid oxidase (LCHAO) is responsible for the formation of methylguanidine, a toxic compound with elevated serum levels in patients with chronic renal failure. Its isozyme glycolate oxidase (GOX), has a role i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8613e13013c09de07980df986f4204af
https://hal.archives-ouvertes.fr/hal-00705285
https://hal.archives-ouvertes.fr/hal-00705285
Autor:
Ylva Lindqvist, Françoise Guéritte, Caroline Vignaud, Jean Marie Bourhis, Florence Lederer, Daniel Guenard, Nicolas Pietrancosta
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2009, 65 (Pt 12), pp.1246-53. ⟨10.1107/S1744309109041670⟩
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2009, 65 (Pt 12), pp.1246-53. ⟨10.1107/S1744309109041670⟩
International audience; Glycolate oxidase, a peroxisomal flavoenzyme, generates glyoxylate at the expense of oxygen. When the normal metabolism of glyoxylate is impaired by the mutations that are responsible for the genetic diseases hyperoxaluria typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87a14ef8b361c2aac233b15b81f1f9ee
https://hal.archives-ouvertes.fr/hal-00769815
https://hal.archives-ouvertes.fr/hal-00769815
Autor:
Jean-Marc Nicaud, Pascale Jolivet, Alain Marty, Chantal Burghoffer, Franck Fudalej, Miguel Cancino, Caroline Vignaud, Thierry Chardot, Florence Bordes, Valérie Dossat
Publikováno v:
FEMS Yeast Research
FEMS Yeast Research, 2007, 7 (8), epub ahead of print. ⟨10.1111/j.1567-1364.2007.00293.x⟩
FEMS Yeast Research, Oxford University Press (OUP), 2007, 7 (8), epub ahead of print. ⟨10.1111/j.1567-1364.2007.00293.x⟩
FEMS Yeast Research, 2007, 7 (8), epub ahead of print. ⟨10.1111/j.1567-1364.2007.00293.x⟩
FEMS Yeast Research, Oxford University Press (OUP), 2007, 7 (8), epub ahead of print. ⟨10.1111/j.1567-1364.2007.00293.x⟩
International audience; Wild-type (WT) Yarrowia lipolytica strain secretes a major extracellular lipase Lip2p which is glycosylated. In silico sequence analysis reveals the presence of two potential N-glycosylation sites (N113IS and N134NT). Strains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::628b1d9d817fb77ec729b3052e427096
https://hal.science/hal-00174139
https://hal.science/hal-00174139
Publikováno v:
Archives of Biochemistry and Biophysics
Archives of Biochemistry and Biophysics, Elsevier, 2007, 465 (2), pp.410-416. ⟨10.1016/j.abb.2007.06.021⟩
Archives of Biochemistry and Biophysics, 2007, 465 (2), pp.410-416. ⟨10.1016/j.abb.2007.06.021⟩
Archives of Biochemistry and Biophysics, Elsevier, 2007, 465 (2), pp.410-416. ⟨10.1016/j.abb.2007.06.021⟩
Archives of Biochemistry and Biophysics, 2007, 465 (2), pp.410-416. ⟨10.1016/j.abb.2007.06.021⟩
Glycolate oxidase, an FMN-dependent peroxisomal oxidase, plays an important role in plants, related to photorespiration, and in animals, where it can contribute to the production of oxalate with formation of kidney stones. The best studied plant glyc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f291700e28da7f60850a920be7c0917
https://hal.archives-ouvertes.fr/hal-02351337
https://hal.archives-ouvertes.fr/hal-02351337