Author |
Alves, Flavio Lopes
![]() ![]() Sallai, Roberto C. ![]() ![]() Salu, Bruno R. ![]() ![]() Miranda, Antonio ![]() ![]() Oliva, Maria Luiza V. ![]() ![]() |
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
Serpin Trypsin Inhibitor Protein Purification Chromatography Human Plasmin InhibitorProteinase-Inhibitors Mechanism Serpins |
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 |
|
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 |
Origin |
|
Access rights | Closed access |
Type | Article |
Web of Science ID | WOS:000387296400014 |
URI | http://repositorio.unifesp.br/handle/11600/49362 |
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