Structural characterization of coagulant Moringa oleifera Lectin and its effect 
on hemostatic parameters

Luz, Luciana de Andrade; Cabral Silva, Mariana Cristina; Ferreira, Rodrigo da Silva; Santana, Lucimeire Aparecida; Silva-Luccao, Rosemeire Aparecida; Mentele, Reinhard; Vilela Oliva, Maria Luiza; Guedes Paiva, Patricia Maria; Breitenbach Barroso Coelho, Luana Cassandra

doi:10.1016/j.ijbiomac.2013.03.044

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Structural characterization of coagulant Moringa oleifera Lectin and its effect on hemostatic parameters

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Mentele, Reinhard
Lottspeich, Friedrich / Protein Analysis, Max Planck Institute of Biochemistry, Max Planck Society;

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引用

Luz, L. d. A., Cabral Silva, M. C., Ferreira, R. d. S., Santana, L. A., Silva-Luccao, R. A., Mentele, R., Vilela Oliva, M. L., Guedes Paiva, P. M., & Breitenbach Barroso Coelho, L. C. (2013). Structural characterization of coagulant Moringa oleifera Lectin and its effect on hemostatic parameters. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 58, 31-36. doi:10.1016/j.ijbiomac.2013.03.044.

引用: https://hdl.handle.net/11858/00-001M-0000-0014-465F-9

要旨

Lectins are carbohydrate recognition proteins. cMoL, a coagulant Moringa oleifera Lectin, was isolated from seeds of the plant. Structural studies revealed a heat-stable and pH resistant protein with 101 amino acids, 11.67 theoretical pI and 81% similarity with a M. oleifera flocculent protein. Secondary structure content was estimated as 46% alpha-helix, 12% beta-sheets, 17% beta-turns and 25% unordered structures belonging to the alpha/beta tertiary structure class. cMoL significantly prolonged the time required for blood coagulation, activated partial thromboplastin (aPTF) and prothrombin times (PT), but was not so effective in prolonging aPTT in asialofetuin presence. cMoL acted as an anticoagulant protein on in vitro blood coagulation parameters and at least on aPTT, the lectin interacted through the carbohydrate recognition domain. (C) 2013 Elsevier B.V. All rights reserved.