Immobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activities

Silva, Mariana C.C.; Santana, Lucimeire A.; Silva-Lucca, Rosemeire A.; Lima, Amanda L.R.; Ferreira, Joana Gasperazzo; Paiva, Patrícia Maria Guedes; Coelho, Luana Cassandra Breitenbach Barroso; Oliva, Maria Luiza Vilela; Zingali, Russolina B.; Correia, Maria T.S.

doi:10.1016/j.procbio.2010.07.017

Cited by 19 publications

(7 citation statements)

References 35 publications

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“…Other lectins also significantly prolongs both coagulation times. Cratylia mollis seed lectin (Cramoll 1,4), a mannose/glucose binding lectin, promotes almost two-fold increase of coagulation times [48]. Bauhinia forficata lectin, BfL, increased only aPTT coagulation time but this effect was not related to human plasma kallikrein or human factor Xa inhibition [49].…”

Section: Cmol Effect On Hemostatic Parametersmentioning

confidence: 99%

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

Luz

Silva

Ferreira

et al. 2013

International Journal of Biological Macromolecules

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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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Section: Cmol Effect On Hemostatic Parametersmentioning

confidence: 99%

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

Luz

Silva

Ferreira

et al. 2013

International Journal of Biological Macromolecules

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“…The CD data are expressed in terms of the mean residue ellipticity [Â] (deg cm 2 dmol −1 ), assuming the protein contains 233 residues. PT, TT and aPTT were determined using a semi-automated BFT II coagulometer (Dade Behring) according to the method of Silva et al [32]. The total plasma was obtained by the centrifugation of several human blood samples at 1726 × g for 15 min (25 • C).…”

Section: Circular Dichroism (Cd)mentioning

confidence: 99%

Purification, primary structure and potential functions of a novel lectin from Bauhinia forficata seeds

Silva

Santana

Mentele

et al. 2012

Process Biochemistry

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A new lectin, BfL, was purified from Bauhinia forficata seeds by ammonium sulfate fractionation, DEAE-Sephadex ion exchange chromatography, Sepharose-4B and chitin affinity chromatographies and Superdex 75 size exclusion chromatography. The molecular homogeneity and purity of BfL were assessed by reversed-phase HPLC. BfL appeared as a single band of approximately 27.0 kDa on SDS-PAGE under non-reducing and reducing conditions, and its molecular weight was determined to be 27,850 Da by LC/ESI-MS. BfL is a glycoprotein with a carbohydrate content of 6.24% determined by the phenol-sulfuric acid method. Fetuin, asialofetuin, thyroglobulin and azocasein inhibited the hemagglutinating activity of BfL, whereas saccharides did not. BfL hemagglutinating activity was stable at 100 • C for 30 min, pHdependent, with the highest activity at pH 6.0, and metal-independent. The primary structure of BfL shows similarity with other lectins from the genus Bauhinia. Deconvolution of the BfL circular dichroism (CD) spectrum indicated the presence of ␣-helix and ␤ structures. BfL increases coagulation time, but this effect is not related to human plasma kallikrein or human factor Xa inhibition. BfL also inhibits ADPand epinephrine-induced platelet aggregation in a dose-dependent manner and is the only currently described lectin from Bauhinia that exhibits anticoagulant and antiplatelet aggregating properties.

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“…A purified soy protein fraction has in vitro platelet anti‐aggregation and anticoagulant activities (Silva et al . ). Integrilin inhibits platelet aggregation in plasma anti‐coagulated with citrate; calcium chelation by citrate increases the inhibitory activity of integrilin (Phillips et al .…”

Section: Resultsmentioning

confidence: 97%

“…Polypeptides from Vipera lebetina venom inhibit platelet aggregation (Barbouche et al 1996); calreticulin, a calciumbinding protein, significantly increases blood coagulation time (Dai et al 1997). A purified soy protein fraction has in vitro platelet anti-aggregation and anticoagulant activities (Silva et al 2011). Integrilin inhibits platelet aggregation in plasma anti-coagulated with citrate; calcium chelation by citrate increases the inhibitory activity of integrilin (Phillips et al 1997).…”

Section: In Vitro Inhibition Of Platelet Aggregation By Modified Hydrmentioning

confidence: 99%

In VitroCalcium-Chelating and Platelet Anti-Aggregation Activities of Soy Protein Hydrolysate Modified by the Alcalase-Catalyzed Plastein Reaction

Zhang

Zhao

2014

Journal of Food Biochemistry

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Soy protein hydrolysate (SPH) (1 mg/mL), generated by alcalase, had a calcium‐chelating activity of 41 mg/g peptide. The alcalase‐catalyzed plastein reaction of SPH was carried out in different media: ethanol–water, methanol–water and water. The effects of SPH and of resulting modified hydrolysates on calcium‐chelating activities and inhibition of calcium precipitation and platelet aggregation were assessed in vitro. The optimum ethanol concentration, alcalase level and reaction temperature for the plastein reaction was 56.8% v/v, 5.26 kU/g peptide and 33.1C, respectively. The modified hydrolysates had better calcium‐chelating activities and stronger inhibition of calcium precipitation and platelet aggregation than SPH. The modified hydrolysate with the highest calcium‐chelating activity showed the strongest inhibitory effects on platelet aggregation and calcium precipitation. The plastein reaction enhances the in vitro calcium‐chelating and platelet anti‐aggregation activities of SPH. Practical Applications In this study, an alcalase‐catalyzed plastein reaction carried out in three media (ethanol–water, methanol–water and water) was used to modify the in vitro calcium‐chelating and platelet anti‐aggregation activities of an alcalase‐generated soy protein hydrolysate. The results revealed that the modified hydrolysates of higher calcium‐chelating activity had stronger inhibitory effects on platelet aggregation and calcium precipitation. The results of this study provide further insight on the enzymatic synthesis of bioactive peptides of higher activity using the plastein reaction.

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Immobilized Cratylia mollis lectin: An affinity matrix to purify a soybean (Glycine max) seed protein with in vitro platelet antiaggregation and anticoagulant activities

Cited by 19 publications

References 35 publications

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

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

Purification, primary structure and potential functions of a novel lectin from Bauhinia forficata seeds

In VitroCalcium-Chelating and Platelet Anti-Aggregation Activities of Soy Protein Hydrolysate Modified by the Alcalase-Catalyzed Plastein Reaction

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