Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.creatorCalderon, Leonardo A-
Autor(es): dc.creatorAlmeida Filho, Humberto A-
Autor(es): dc.creatorTeles, Rozeni C. L-
Autor(es): dc.creatorMedrano, Francisco J-
Autor(es): dc.creatorBloch Jr, Carlos-
Autor(es): dc.creatorSantoro, Marcelo M-
Autor(es): dc.creatorFreitas, Sonia M-
Data de aceite: dc.date.accessioned2021-10-14T18:07:20Z-
Data de disponibilização: dc.date.available2021-10-14T18:07:20Z-
Data de envio: dc.date.issued2017-12-07-
Data de envio: dc.date.issued2017-12-07-
Data de envio: dc.date.issued2010-
Fonte completa do material: dc.identifierhttp://repositorio.unb.br/handle/10482/27891-
Fonte completa do material: dc.identifierhttps://dx.doi.org/10.1590/S1677-04202010000200001-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/capes/624005-
Descrição: dc.descriptionInga cylindrica Trypsin Inhibitor (ICTI) was purified as a single polypeptide chain by one step anion-exchange chromatography from a crude extract of Inga cylindrica (Vell.) Mart. seeds. ICTI is a 19.5 kDa protein presenting a remarkable inhibitory activity against bovine trypsin (EC 3.4.21.4) (Ki = 4.3 nM). Circular dichroism analysis revealed that this inhibitor is a β type protein (40.4% of β-strand; 24.6% of β-turn and 6.7% of α-helix) in accordance with properties displayed in Kunitz type inhibitors. ICTI is a thermal stable protein within a wide range of pH (1.6 to 10.0) exhibiting highest stability at pH 7.0 as indicated by Tm of 70.0 ºC and ΔG25 of 48.5 ± 0.7 kJ.mol-1. The values of ΔG25 at pH 1.6 (22.5 ± 1.2 kJ.mol-1) and pH 10.0 (31.5 ± 1.0 kJ.mol-1) indicate a reduced structural stability of the protein under these conditions. This is likely to result from pKa differences of the acid and basic side chains reflecting the changes in the non-covalent interactions in the folded state.-
Formato: dc.formatapplication/pdf-
Idioma: dc.languageen-
Publicador: dc.publisherBrazilian Journal of Plant Physiology-
Direitos: dc.rightsAcesso Aberto-
Palavras-chave: dc.subjectInga cylindrica [Vell.] Mart-
Palavras-chave: dc.subjectLeguminosae-
Palavras-chave: dc.subjectMimosoideae-
Palavras-chave: dc.subjectprotease inhibitor-
Palavras-chave: dc.subjectprotein stability-
Palavras-chave: dc.subjecttrypsin inhibitor-
Título: dc.titlePurification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds-
Tipo de arquivo: dc.typelivro digital-
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