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• W1996545946 abstract "A 189-bp sequence was isolated from the hyperthermophilic archaeon Thermococcus chitonophagus and was found to present strong homology with a large number of chitinase genes from a variety of organisms and particularly with the chitinaseA gene from Pyrococcus kodakaraensis (Pk-chiA). This fragment was subcloned to an expression vector and overexpressed in Escherichia coli. The E. coli BLR21(DE3)pLysS transformant, harbouring the gene on the pET-31b plasmid vector, was found to overproduce the target protein at high levels. The 63 aminoacid-long peptide was efficiently purified to homogeneity, with a one-step, semi-denaturing affinity chromatography, on a metal chelation resin and was used for the production of a specific, polyclonal antibody from rabbits. The produced antibody was demonstrated to display strong and specific affinity for the chitinase A from Serratia marcescens (Sm-chiA), as well as the membrane-bound chitinase70 from Thermococcus chitonophagus (Tc-Chi70). The strong sequence homology, in combination with the demonstrated specific immunochemical affinity, indicates that the isolated peptide is part of a chitinolytic enzyme of T. chitonophagus. In particular, it could belong to the membrane-bound chi70, or to a distinct chitinase, coded by a different gene, or even by the same gene, following post-transcriptional or post-translational modifications." @default.
• W1996545946 created "2016-06-24" @default.
• W1996545946 creator A5005415469 @default.
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• W1996545946 date "2004-06-01" @default.
• W1996545946 modified "2023-09-23" @default.
• W1996545946 title "Isolation, cloning, and overexpression of a chitinase gene fragment from the hyperthermophilic archaeon Thermococcus chitonophagus: semi-denaturing purification of the recombinant peptide and investigation of its relation with other chitinases" @default.
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• W1996545946 doi "https://doi.org/10.1016/j.pep.2004.02.002" @default.
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