Literature DB >> 15922393

Procoagulant activity of Calotropis gigantea latex associated with fibrin(ogen)olytic activity.

R Rajesh1, C D Raghavendra Gowda, A Nataraju, B L Dhananjaya, K Kemparaju, B S Vishwanath.   

Abstract

The latex of Calotropis gigantea is a rich source of useful components that has medicinal properties and one of the main applications is in controlling bleeding. The crude latex extract contained many proteins, which are highly basic in nature and exhibited strong proteolytic activity. The crude extract hydrolyses casein, human fibrinogen and crude fibrin clot in a dose-dependent manner. The hydrolyzing activity was completely inhibited by IAA indicating they belong to the super family, cysteine proteases. Crude extract hydrolyses Aalpha, Bbeta and gamma subunits of fibrinogen. Among all the subunits the preferential subunit to get hydrolyzed was Aalpha followed by Bbeta and gamma subunit is highly resistant and hydrolyzed at higher protein concentration or over a prolonged incubation time. The crude extract hydrolysis crude fibrin clot strongly compared to trypsin and papain. Pharmacologically the crude extract is hemorrhagic and induces skin hemorrhage at >75 microg and reduces the coagulation time of citrated plasma from 150 to 47 s and promotes blood coagulation. Procoagulation and blood clot hydrolysis are important in wound healing process. This is due to unique cysteine proteases of plant latex and is responsible for the pharmacological actions observed in folk medicine.

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Year:  2005        PMID: 15922393     DOI: 10.1016/j.toxicon.2005.03.012

Source DB:  PubMed          Journal:  Toxicon        ISSN: 0041-0101            Impact factor:   3.033


  15 in total

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10.  Purification, characterization and fibrino(geno)lytic activity of cysteine protease from Tabernaemontana divaricata latex.

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Journal:  3 Biotech       Date:  2021-01-31       Impact factor: 2.406

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