Ecarin is a snake venom (Echis carinatus) that directly activates prothrombin to meizothrombin This action is not dependent on phospholipid membranes and . Objective(s): Echis carinatus is one of the venomous snakes in Iran. The venom of Iranian Echis carinatus is a rich source of protein with various factors affecting . In this research, the effects of Echis carinatus crude venom and its fractions on mice were analyzed. Moreover, the results of coagulation tests.

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In vivo evaluation of homeostatic effects of Echis carinatus snake venom in Iran

Source of Venoms The venom of E. Authentication and the taxonomic identification of plant materials was confirmed by Dr. Purification and partial characterization of a coagulant serine protease from the venom of cariatus Iranian snake Agkistrodon halys.

Snake venom serine proteinases: F 1 ion exchange chromatography carinatuus to the formation of eight subfractions F 1 A to F 1 H.

They move about mainly by sidewinding: Compared with the normal time, this interval is lower, showing the intense coagulation properties of these subfractions.

Although Hibiscus aethiopicus L. However, haemorrhage induction was significantly reduced and or fully neutralised with the increase of the extract concentration and time, in contrast with the preincubation assay represented by Figure 1. In any case, antivenin therapy and intravenous hydration within hours of the bite are vital for survival. Identification, purification and properties of a prothrombin activator.


Coagulant activity Normal plasma comprised mixed samples from 20 healthy donors.

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Interestingly in this study we found that the extract can inhibit dose carinafus the procoagulant activity of the E. Step Protein Venom Echis reveal substantial intra-family gene diversity and novel venom transcripts. Finally, by comparing the fibrinogen time after subfraction injections and normal test time, we can infer intense activation of coagulation cascade and fibrin production.

The subfractions were pooled and dialyzed like in gel chromatography. Recombinant snake venom prothrombin activators. In this research, the effects of Echis carinatus crude venom and its fractions on mice were analyzed. Countries India, Sri Lanka. The inset shows the dose-dependent procoagulant activity of E.

The belly is whitish to pinkish, uniform in color or with brown dots that are either faint or distinct. The mechanism of activation of bovine prothrombin by an activator isolated from Echis carinatus venom and characterization of the new active intermediates.

Halys agkistrodon snake venom was analyzed by Ghorbanpur et al. Procoagulant proteins snake venoms.

Snake venom of Echis carinatus sochureki

For example, Gao et al. Inhibition of procoagulant activity.

An hour after the injection of F 1 B, blood samples were collected. The subcaudals are undivided and numberand the anal scale is single.


Clinical evidence from an authenticated case snzke. The venom from this species is used in the manufacture of several drugs. Purification and characterization of a prothrombin activator from the venom of the Australian brown snake, Pseudonaja textilis textilis.

This rapid response of the coagulation cascade occurs in the animal body caeinatus generates clinical effects such as coagulopathy, which may provoke death. Isolation of subfractions F 1 using Ion exchange chromatography Among carrinatus fractions obtained from gel chromatography fraction F 1 was selected dnake furhter isolation because of its lower coagulation time, and was taken to the DEAE-Sepharose ion exchange column.

Often, they are most active after rains or on humid nights. The molecular weight of this purified fraction was approximately estimated to be 56 kDa Figure 4C. Morita T, Iwanga S. The MED was found to be 7. According to the Figure 4Ca single band of F 1 B 4 indicates the purity of this protein.

Almost all patients develop oliguria or anuria within a few hours to as late as 6 days post bite.

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