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- Title
Purification and partial characterization of a novel lectin from Dioclea lasiocarpa Mart seeds with vasodilator effects.
- Authors
do Nascimento, Antônia Sâmia F.; Gondim, Ana Cláudia S.; Cajazeiras, João B.; Correia, Jorge Luis A.; Pires, Alana de F.; do Nascimento, Kyria S.; Silva, André Luis C.; Nagano, Celso S.; Assreuy, Ana Maria S.; Cavada, Benildo S.
- Abstract
A lectin from seeds of Dioclea lasiocarpa (DLL) was purified in a single step by affinity chromatography in a Sephadex G-50 column. DLL haemagglutinated rabbit erythrocytes showing stability even after 1 h of exposure to a different pH values (optimal between pH 6.0 and 8.0) but was inhibited after incubation with d-mannose and d-glucose. The pure protein possessed a molecular weight of 25 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis and 25,410Da by mass spectrometry. The results analyzed by the software SELCON 3 indicate that β-sheet secondary structures are predominant in DLL (approximately 40.2% antiparallel β-sheet, 4.6% parallel β-sheet, 7.2% α-helices, 17.3% turns, and 28.7% unordered structures). Mechanical activity of isolated aorta from rat measured by cumulative concentration curves of DLL, performed at the contraction plateau induced by phenylephrine in either endothelium-intact or denuded aorta. DLL (IC50 = 34.12 ± 3.46 µg/ml) relaxed precontracted endothelized aortic rings by 34.61 ± 9.06%, 55.19 ± 11.9%, and 81.33 ± 14.35%, respectively, at 10 µg/ml (initial concentration), 30 µg/ml, and 100 µg/ml (maximum effect). All effects occurred via interaction with lectin domains and participation of nitric oxide. Copyright © 2012 John Wiley & Sons, Ltd.
- Publication
Journal of Molecular Recognition, 2012, Vol 25, Issue 12, p657
- ISSN
0952-3499
- Publication type
Article
- DOI
10.1002/jmr.2222