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

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78389

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

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Luz, L. d. A., Cabral Silva, M. C., Ferreira, R. d. S., Santana, L. A., Silva-Luccao, R. A., Mentele, R., et al. (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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-465F-9
Abstract
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.