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

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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Luz Lde A,Silva MC,Ferreira Rda S,Santana LA,Silva-Lucca RA,Mentele R,Oliva ML,Paiva PM,Coelho LC

doi

10.1016/j.ijbiomac.2013.03.044

subject

Has Abstract

pub_date

2013-07-01 00:00:00

pages

31-6

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(13)00130-X

journal_volume

58

pub_type

杂志文章

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