"RIV/00216224:14310/08:00024871!RIV10-MSM-14310___" . . "CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA"@en . . "2008-01-01+01:00"^^ . "P(GA303/06/0570), P(LC06030)" . "Lectin; Burkholderia cenocepacia; SPR; ITC"@en . "Imberty, Anne" . "978-80-210-4526-2" . . "Imberty, Anne" . . "14310" . "CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA" . . "Delia, Monia" . . . . . "XII. Setk\u00E1n\u00ED biochemik\u016F a molekul\u00E1rn\u00EDch biolog\u016F" . "CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA" . . "Four genes coding proteins homologous to lectin PA-IIL from Pseudomonas aeruginasa have been found in the genome of B. cenocepacia. One of them, named BclC, is a 28 kDa protein which is able to recognize D-mannosylated carbohydrates. This protein also exhibits partial sequence homology with the protein CV-IIL from the Chromobacterium violaceum. BclC has been cloned and prepared in recombinant form. Sequence analysis showed two distinct domains in the protein, N-terminal part that does not have any sequence homolog in genomic and protein databases, and C-terminal part that codes for lectin domain. Both domains were also cloned separately to simplify further structure-function characterization. Detailed functional studies using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters." . "CHARACTERISATION OF A NEW LECTIN BCLC FROM THE HUMAN OPPORTUNISTIC PATHOGEN BURKHOLDERIA CENOCEPACIA"@en . . . "Kostl\u00E1nov\u00E1, Nikola" . "Delia, Monia" . . "Brno" . "Four genes coding proteins homologous to lectin PA-IIL from Pseudomonas aeruginasa have been found in the genome of B. cenocepacia. One of them, named BclC, is a 28 kDa protein which is able to recognize D-mannosylated carbohydrates. This protein also exhibits partial sequence homology with the protein CV-IIL from the Chromobacterium violaceum. BclC has been cloned and prepared in recombinant form. Sequence analysis showed two distinct domains in the protein, N-terminal part that does not have any sequence homolog in genomic and protein databases, and C-terminal part that codes for lectin domain. Both domains were also cloned separately to simplify further structure-function characterization. Detailed functional studies using surface plasmon resonance (SPR) and isothermal titration calorimetry (ITC) allowed to define binding properties (afinity, kinetics) and thermodynamic parameters."@en . "Brno" . . "Wimmerov\u00E1, Michaela" . . "5"^^ . . "[E5587081D1E8]" . "RIV/00216224:14310/08:00024871" . . . "Masarykova univerzita" . "5"^^ . . "\u0160ul\u00E1k, Ond\u0159ej" . "2"^^ . . "359542" .