Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Christian Gaudin"'
Autor:
Chantal Tardif, Christian Gaudin, Sandrine Pagès, Anne Belaich, Laurent Gal, Jean-Pierre Belaich
Publikováno v:
Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
Journal of Bacteriology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
Journal of Bacteriology, American Society for Microbiology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
Journal of Bacteriology, 1997, 179 (21), pp.6595-6601. ⟨10.1128/jb.179.21.6595-6601.1997⟩
International audience; The gene coding for CelG, a family 9 cellulase from Clostridium cellulolyticum, was cloned and overexpressed in Escherichia coli. Four different forms of the protein were genetically engineered, purified, and studied: CelGL (t
Autor:
C Reverbel-Leroy, Christian Gaudin, Alain Bernadac, Anne Belaich, Chantal Tardif, Jean-Pierre Belaich
Publikováno v:
Microbiology. 142:1013-1023
The CelF-encoding sequence was isolated from Clostridium cellulolyticum genomic DNA using the inverse PCR technique. The gene lies between cipC (the gene encoding the cellulosome scaffolding protein) and celC (coding for the endoglucanase C) in the l
Autor:
Christian Gaudin, Anne Belaich, M Loutfi, Henri-Pierre Fierobe, Eric Faure, Chantal Bagnara, Daniel Baty, Jean-Pierre Belaich
Publikováno v:
Journal of Bacteriology. 173:7956-7962
A construction was carried out to obtain a high level of expression in Escherichia coli of the gene celCCA, coding for the endoglucanase A from Clostridium cellulolyticum (EGCCA). The enzyme was purified in two forms with different molecular weights,
Autor:
Chantal Bagnara-Tardif, Christian Gaudin, Françoise Guerlesquin, Henri-Pierre Fierobe, Paul Sauve, Jean-Pierre Belaich, Anne Belaich
Publikováno v:
European journal of biochemistry. 217(2)
An Escherichia coli clone was constructed to overproduce endoglucanase C (CelCCC) from Clostridium cellulolyticum. This construction made it easier to isolate the enzyme but, as observed in the case of endoglucanase A (CelCCA) from the same organism,
Publikováno v:
Biochimie. 62:741-746
Resume Le comportement, en fonction de la temperature, de la proteine periplasmique d' Escherichia coli , affine pour la leucine, l'isoleucine et la valine, a ete etudie. Les variations d'affinite de la proteine pour la leucine sous l'influence de la
Publikováno v:
Biochemical and biophysical research communications. 86(4)
The enthalpy variation (ΔH) induced by addition of glutamine to glutamine binding protein isolated from E. coli has been studied by microcalorimetry. The reaction was very exothermic. The free energy variation (ΔG) was calculated from the dissociat