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Título: Purification and structural stability of a trypsin inhibitor from Amazon Inga cylindrica [Vell.] Mart. seeds
Autor(es): Calderon, Leonardo A
Almeida Filho, Humberto A
Teles, Rozeni C. L
Medrano, Francisco J
Bloch Jr, Carlos
Santoro, Marcelo M
Freitas, Sonia M
Assunto: Inga cylindrica [Vell.] Mart
Leguminosae
Mimosoideae
protease inhibitor
protein stability
trypsin inhibitor
Data de publicação: 2010
Editora: Brazilian Journal of Plant Physiology
Referência: Braz. J. Plant Physiol.,v.22,n.2,p.73-79,2010
Resumo: Inga 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.
Unidade Acadêmica: Em processamento
DOI: https://dx.doi.org/10.1590/S1677-04202010000200001
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