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The recombinant plant Bauhinia bauhinioides elastase inhibitor reduces rat thro...
Oliveira, Cleide; Valois, Mayara Vioto; Ottaiano, Tatiana Fontes; Miranda, Antonio; Hansen, Daiane; Sampaio, Misako Uemura; Oliva, Maria Luiza VilelaMade available in DSpace on 2022-04-29T08:30:14Z (GMT). No. of bitstreams: 0 Previous issue date: 2021-12-01; The anti-inflammatory effects of the plant protease inhibitor BbCI (Bauhinia bauhinioides cruzipain inhibitor), which blocks elastase, cathepsin G, and L, and proteinase 3 has been demonstrated. Here, we investigated the recombinant rBbCI-His(6) (containing a histidine tail) in an experimental venous th...
Purification of a lectin with antibacterial activity from Bothrops leucurus sna...
Nunes, Erika dos Santos; Souza, Mary Angela Aranda de; Vaz, Antônio Fernando de Melo; Santana, Giselly Maria de Sá; Gomes, Francis SoaresAcesso restrito: Texto completo. p. 57-63.; Submitted by JURANDI DE SOUZA SILVA (jssufba@hotmail.com) on 2012-02-24T12:27:40Z No. of bitstreams: 1 __pdn.sciencedirect.com_....0-S109649591100039X-main.pdf: 285488 bytes, checksum: eb5db11aed712ad4983cbc91c31fc451 (MD5); Made available in DSpace on 2012-02-24T12:27:40Z (GMT). No. of bitstreams: 1 __pdn.sciencedirect.com_....0-S109649591100039X-main.pdf: 285488 byt...
The defensive functions of plant inhibitors are not restricted to insect enzyme...
Oliva, Maria Luiza Vilela
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor
Hansen, Daiane; Macedo-Ribeiro, Sandra; Veríssimo, Paula; Yoo Im, Sonia; Sampaio, Misako Uemura; Oliva, Maria Luiza VilelaBauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine prot...