Purification and biochemical characterization of Eumiliin from Euphorbia milii var. hislopii latex

Fonseca, Kelly Cortes; Morais, Nadia Cristina Gomes de; Queiroz, Mayara Ribeiro de; Silva, M.C.; Gomes, Marcos Antônio Silvestre; Costa, Júnia de Oliveira; Mamede, Carla Cristine Neves; Torres, Fernanda Silva; Penha-Silva, Nilson; Beletti, Marcelo Emı́lio; Canabrava, Hudson Armando Nunes; Oliveira, Fábio de

doi:10.1016/j.phytochem.2010.02.009

Cited by 52 publications

(33 citation statements)

References 40 publications

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“…An enzyme isolated from the latex of Euphorbia milii var. hislopii has 30-kDa molecular mass and is called Eumiliin [24]. The plant protease has 26-kDa molecular mass isolated from C. Melo L. [10] These plant proteases are similar with the present study.…”

Section: Resultssupporting

confidence: 87%

Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

Nadaroğlu

Demir

2012

Eur Food Res Technol

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In this research, a protease from the compositae (Scorzonera hispanica L.) was extracted and puriWed through (NH 4 ) 2 SO 4 precipitation, CM-Sephadex and Sephacryl S200. At the end of puriWcation by gel Wltration on a Sephacryl S-200 column, 87.11-fold puriWcation was achieved. It was shown that puriWed enzyme was homogeneous in terms of SDS-PAGE with molecular mass estimate of 30 kDa. The enzyme named compositain depicted an optimal pH of 8.0 and was stable at pH 7.0-9.0, and its optimal temperature was at 50°C. While Tween 80 (0.2 %) was activated to the puriWed protease enzyme, it was partially inhibited by 5 mM concentration of some metal salts and EDTA, PMSF, dithiothreitol, H 2 O 2 and -mercaptoethanol. The enzyme activity was stable even in the presence of detergents and organic solvents. In addition, it was investigated whether the puriWed and characterized protease enzyme would cause to congeal milk. As a result, it was determined that the compositain could congeal milk and it would be used for cheese production. The compositain had potential application in food processing.

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Section: Resultssupporting

confidence: 87%

Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

Nadaroğlu

Demir

2012

Eur Food Res Technol

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“…In this sense, Siritapetawee et al [14] have proposed the potential use of AMP48 (a serine protease from Artocarpus heterophyllus) as antithrombotic for treatment thromboembolic disorders such as strokes, pulmonary embolism and deep vein thrombosis. Additionally, Fonseca et al [15] have purified and characterized a serine protease with fibrinogenolytic activity from Euphorbia milii latex. The potential use in medicinal treatment, for example for thrombosis has been suggested for a serine protease with fibrinogenolytic activity and high stability from Euphorbia cf.…”

Section: Introductionmentioning

confidence: 99%

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

et al. 2016

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a b s t r a c tPlant serine proteases have been widely used in food science and technology as well as in medicine. In this sense, several plant serine proteases have been proposed as potential anti-coagulants and antiplatelet agents. Previously, we have reported the purification and identification of a plant serine protease from Solanum tuberosum leaves. This potato enzyme, named as StSBTc-3, has a molecular weight of 72 kDa and it was characterized as a subtilisin like protease. In this work we determine and characterize the biochemical and medicinal properties of StSBTc-3. Results obtained show that, like the reported to other plant serine proteases, StSBTc-3 is able to degrade all chains of human fibrinogen and to produces fibrin clot lysis in a dose dependent manner. The enzyme efficiently hydrolyzes b subunit followed by partially hydrolyzed a and g subunits of human fibrinogen. Assays performed to determine StSBTc-3 substrate specificity using oxidized insulin b-chain as substrate, show seven cleavage sites: Asn3-Gln4; Cys7-Gly8; Glu13-Ala14; Leu15-Tyr16; Tyr16-Leu17; Arg22-Gly23 and Phe25-Tyr26, all of them were previously reported for other serine proteases with fibrinogenolytic activity. The maximum StSBTc-3 fibrinogenolytic activity was determined at pH 8.0 and at 37 C. Additionally, we demonstrate that StSBTc-3 is able to inhibit platelet aggregation and is unable to exert cytotoxic activity on human erythrocytes in vitro at all concentrations assayed. These results suggest that StSBTc-3 could be evaluated as a new agent to be used in the treatment of thromboembolic disorders such as strokes, pulmonary embolism and deep vein thrombosis.

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“…hislopii (Euphorbiaceae) hydrolyzes fibrinogen in vitro. [148] All these findings support the traditional use of plant latex for wound healing. [145][146][147] Whether the fibrinolytic properties of all these proteases from plant latices, except those of the Asclepiadaceae, are based on plasminogen activator activity or a plasmin-like activity isn't proved yet.…”

Section: Plant Proteasesmentioning

confidence: 62%

Serine-proteases as plasminogen activators in terms of fibrinolysis

Flemmig

Melzig

2012

Journal of Pharmacy and Pharmacology

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Objectives This review should give an overview about the natural human plasminogen activators and their various modified variants as well as similar substances isolated from animals, microorganisms and plants. When a blood clot is formed in a blood vessel, it avoids the oxygen supply of the surrounding tissue. A fast fibrinolytic therapy should redissolve the blood vessel and reduce the degradation of the tissue. All proteases that are part of the human blood coagulation and fibrinolytic system belong to the serine protease family. t-PA (tissue plasminogen activator) and u-PA (urokinase plasminogen activator) are the naturally occurring fibrinolytic agents that are also used in therapy. Key findings Despite many years of research, t-PA is still the gold standard in fibrinolytic therapy. But it has to be given as an infusion, which needs time. Modified fibrinolytic substances are, were, or perhaps will be in the market. They have different advantages over t-PA, but often the disadvantages predominate. Conclusion Many substances have been developed but an optimal fibrinolytic agent combined with a simple administration is not in therapeutic use to date.

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Purification and biochemical characterization of Eumiliin from Euphorbia milii var. hislopii latex

Cited by 52 publications

References 40 publications

Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

Purification and characterization of a novel serine protease compositain from compositae (Scorzonera hispanica L.)

Fibrin(ogen)olytic and antiplatelet activities of a subtilisin-like protease from Solanum tuberosum (StSBTc-3)

Serine-proteases as plasminogen activators in terms of fibrinolysis

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