Identification and characterisation of serine protease inhibitors from araucaria angustifolia seeds

Identification and characterisation of serine protease inhibitors from araucaria angustifolia seeds

Author Alves, Flavio Lopes Autor UNIFESP Google Scholar
Sallai, Roberto C. Autor UNIFESP Google Scholar
Salu, Bruno R. Autor UNIFESP Google Scholar
Miranda, Antonio Autor UNIFESP Google Scholar
Oliva, Maria Luiza V. Autor UNIFESP Google Scholar
Abstract Araucaria angustifolia seeds are characterised by a relatively high content of starch and protein. This study aimed to verify the presence of -amylase inhibitors in the seeds and to characterise a trypsin inhibitor found in the embryo tissues. Inhibitor purification was carried out by the saline extraction of proteins, acetone precipitation and affinity chromatography. Two protein bands of molecular weight estimated by SDS-PAGE at about 35kDa were further examined by high-performance liquid chromatography coupled to a mass spectrometer and were shown to be 36.955Da (AaTI-1) and 35.450Da (AaTI-2). The sequence of the N-terminal region shows that AaTI-1 and AaTI-2 are structurally similar to plant inhibitors of the serpin family. A mixture of AaTI-1 and AaTI-2, identified as AaTI, shows selectivity for the inhibition of trypsin (K-iapp 85nM) and plasmin (K-iapp 7.0M), but it does not interfere with the chymotrypsin, human plasma kallikrein, porcine kallikrein or other coagulation enzymes activity. [GRAPHICS] .
Keywords Araucaria Angustifolia
Trypsin Inhibitor
Protein Purification
Human Plasmin InhibitorProteinase-Inhibitors
Language English
Sponsor Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) [2009/53799-5]
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)
Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
Grant number FAPESP: 2009/53799-5
Date 2016
Published in Natural Product Research. Abingdon, v. 30, n. 23, p. 2712-2715, 2016.
ISSN 1478-6419 (Sherpa/Romeo, impact factor)
Publisher Assoc Medica Brasileira
Extent 2712-2715
Access rights Closed access
Type Article
Web of Science ID WOS:000387296400014

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