Journal
NATURAL PRODUCT RESEARCH
Volume 30, Issue 23, Pages 2712-2715Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/14786419.2015.1136887
Keywords
Araucaria angustifolia; serpin; trypsin inhibitor; protein purification; chromatography; human plasmin inhibitor
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Funding
- 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)
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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] .
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