2012
DOI: 10.1002/ptr.4663
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Effects of Mucuna pruriens Protease Inhibitors on Echis carinatus Venom

Abstract: The medicinal plant Mucuna pruriens, with reputed anti-snake venom properties has been reported to contain a kunitz-type trypsin inhibitor. This study was undertaken to further evaluate the protease inhibitory potential of gpMuc, a multiform glycoprotein, and other protein fractions from M. pruriens seeds against trypsin, chymotrypsin, Echis carinatus snake venom, ecarin and thrombin. The results showed that gpMuc inhibited both trypsin and chymotrypsin activities and was thermally stable, maintaining its tryp… Show more

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Cited by 4 publications
(2 citation statements)
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“…One of the proteins present in the seed extract is a multiform glycoprotein (gpMuc) of apparent molecular mass 20 -28 kDa. N-terminal sequences of seven glycosylated isoforms of this protein show the conserved signature sequence of Kunitz-type protease inhibitors (27,28). This protein can inhibit proteolytic components of snake venom and thus may provide direct protection against the toxic effects of snakebite.…”
mentioning
confidence: 99%
“…One of the proteins present in the seed extract is a multiform glycoprotein (gpMuc) of apparent molecular mass 20 -28 kDa. N-terminal sequences of seven glycosylated isoforms of this protein show the conserved signature sequence of Kunitz-type protease inhibitors (27,28). This protein can inhibit proteolytic components of snake venom and thus may provide direct protection against the toxic effects of snakebite.…”
mentioning
confidence: 99%
“…Furthermore, it has been reported to stimulate the synthesis of antibodies capable of cross-reacting with venomous proteins and inhibits the venom proteolytic apparatuses, thus mitigating toxicity (Guerranti et al, 2004;Kumar et al, 2016). This immunogenic glycoprotein (gpMuc) has a molecular weight of 20.3 to 28.7 kDa and pI of 4.8 to 6.5 (Di Patrizi et al, 2006;Hope-Onyekwere, 2012) and has Seven (7) different N-terminal isoforms, some of which possess structural similarities to PLA2 of venoms (Lucia et al, 2012). Recent investigations by Kumar et al (2016) substantiated that a specific purified protein from M. pruriens code-named MP-4 (20.9 kDa) reacts with antibodies against Echiscarinatus venom, though contrarily, the MP-4 protein exhibited no direct protease inhibitory action.…”
Section: The Plants Used Against Snakebite and Envenomation In Sub-sa...mentioning
confidence: 99%