Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Archara Vongsuwan"'
Publikováno v:
FEBS Journal. 272:3376-3386
The enzymatic properties of chitinase A from Vibrio carchariae have been studied in detail by using combined HPLC and electrospray MS. This approach allowed the separation of α and β anomers and the simultaneous monitoring of chitooligosaccharide p
Autor:
Wipa Suginta, Robert Robinson, Archara Vongsuwan, Chomphunuch Songsiriritthigul, Jirundon Yuvaniyama, Heino Prinz
Publikováno v:
Acta Crystallographica Section F-Structural Biology and Crystallization Communications
Chitinase A of Vibrio carchariae was expressed in Escherichia coli M15 host cells as a 575-amino-acid fragment with full enzymatic activity using the pQE60 expression vector. The yield of the highly purified recombinant protein was approximately 70 m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cad69efd1c4b80792bf8ee5ff295455e
https://europepmc.org/articles/PMC1991324/
https://europepmc.org/articles/PMC1991324/
Autor:
Wipa, Suginta, Archara, Vongsuwan, Chomphunuch, Songsiriritthigul, Jisnuson, Svasti, Heino, Prinz
Publikováno v:
The FEBS journal. 272(13)
The enzymatic properties of chitinase A from Vibrio carchariae have been studied in detail by using combined HPLC and electrospray MS. This approach allowed the separation of alpha and beta anomers and the simultaneous monitoring of chitooligosacchar
Autor:
Archara Vongsuwan, Wipa Suginta, Heino Prinz, Chomphunuch Songsiriritthigul, Jisnuson Svasti, Linda A. Fothergill-Gilmore, Rory R. Duncan, Peter Estibeiro
Publikováno v:
Archives of biochemistry and biophysics. 424(2)
We provide evidence that chitinase A from Vibrio carchariae acts as an endochitinase. The chitinase A gene isolated from V. carchariae genome encodes 850 amino acids expressing a 95-kDa precursor. Peptide masses of the native enzyme identified from M