AI Article Synopsis
- Lectins are proteins that recognize carbohydrates, and cMoL is a specific lectin extracted from Moringa oleifera seeds known for its potential anticoagulant properties.
- Structural analysis shows that cMoL has 101 amino acids, is stable under heat and varying pH, and shares high similarity with another Moringa protein, featuring a complex secondary structure.
- cMoL significantly delays blood coagulation times in certain tests, indicating its role as an anticoagulant, but its effectiveness may be reduced in the presence of specific glycoproteins.
Article 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% α-helix, 12% β-sheets, 17% β-turns and 25% unordered structures belonging to the α/β tertiary structure class. cMoL significantly prolonged the time required for blood coagulation, activated partial thromboplastin (aPTT) 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.
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| http://dx.doi.org/10.1016/j.ijbiomac.2013.03.044 | DOI Listing |
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