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.
|Published (Last):||5 December 2008|
|PDF File Size:||7.32 Mb|
|ePub File Size:||14.33 Mb|
|Price:||Free* [*Free Regsitration Required]|
There was a problem providing the content you requested
Subfractions of F 1 ; C: Animals showed normal body weight increase during the two weeks period. Support Center Support Center. This page was last edited on 23 Decemberat How to interpret and pursue sna,e abnormal prothrombin time, activated partial thromboplastin time, and bleeding time in adults.
Regarding the PT test results, subfractions F 1 A mean 6. 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.
Snake venom of Echis carinatus sochureki
Purification and partial characterization of a coagulant serine protease from the venom of the Iranian snake Agkistrodon halys. It may be suggested that with low amount of total protein the PT value decreases. The objective of the study is to investigate the anti-snake venom activities of a local plant, Hibiscus aethiopicus L. This venom is very toxic causing severe tissue and organ damage. Often ecbis in small hills and scrub jungles. First aid for bites by Viperid snakes likely to cause significant local injury at the bite site see listing in Comments section.
Approaching the golden age of natural product pharmaceuticals from venom libraries: A novel prothrombin activator from the venom of Micropechis ikaheka: Head scales are keeled. Table of Contents Alerts. The supernatant was filtered on carinztus 0.
Many will be terrified, fearing sudden death and, in this mood, they may behave irrationally or even hysterically. Our observation showed that the molecular weight of F 1 B 4 is vfnom to prothrombin activator enzymes which have been already reported Snake venoms and the hemostatic system.
Snake venom of Echis carinatus sochureki – Latoxan
The present study aims to study the antisnake venom activity of a local plant, Hibiscus aethiopicus L. All guinea pigs when treated with venoms E. Once fibrinogen is removed from the blood, its viscosity evhis decrease and the blood circulation will be optimized. Lower lateral body scales are markedly serrated.
The mechanism of activation of bovine prothrombin by an activator isolated from Echis carinatus venom and characterization of the new active intermediates. Any single snake species may possess toxins that act in one or more of these categories, though rarely all six.
Accessed 12 September However, under in vitro conditions, this venom will generate high coagulation which is due to activation of the prothrombin. Now, it may be used as a rich source of proteins that may be employed in the pharmaceutical industry. Evaluations of Acute Toxicity of H. The total protein of crude venom is Conclusion Protein with coagulation activities was purified from the venom of E.
Isolation and purification of coagulation factors Isolation and purification of coagulation factors were performed using 50 mg of Ec crude venom using a combination of gel chromatography and ion exchange chromatography. Isolation and purification of coagulation factors were performed using 50 mg of Ec crude venom using a combination of gel chromatography and ion exchange chromatography.
In vivo evaluation of homeostatic effects of Echis carinatus snake venom in Iran
B Chart showing oral administrations of the H. The mean PT before injection was Discussion It has been important for scientists to identify and study the compounds in snake venom.
For isolation, identification and investigation of the properties of Ec crude venom coagulation factors, a combination of gel chromatography and ion exchange chromatography was employed. Insights into the disintegrin gene family. However, the rate of activation is five orders of magnitude lower than the activation by prothrombinase complex 12and the mechanism of cleavage proceeds through prethrombin-2 rather than through meizothrombin Besides FXa, these enzymes act independently, eliminating the use of any cofactors, including FV, on carboxilated or nonocarboxilated prothrombin.
Mouse blood samples were centrifuged for ten minutes at 3, rpm. Among the fractions obtained from gel chromatography fraction F 1 was selected for furhter isolation because of its lower coagulation time, and was taken to the DEAE-Sepharose ion exchange column.
Although an intravenous administration of antivenom, prepared from IgG of venomimmunised horses or sheep, is an effective treatment for systemic envenoming, the clinical consensus is that antivenom is of limited effectiveness against the effects of local envenoming that develop rapidly after a bite. In contrast to our results reported in the previous work [ 17 ], the oral route when compared to a general acute toxicity index showed normal with no extraordinary symptoms as well as no acute toxicity.
In another work, Agkistrodon acutus snake venom was exposed to ion exchange chromatography with Sepharose DEAE followed by gel chromatography on Sephacryl S to isolate fractions with coagulation activities [ 25 ]. All guinea pigs treated with venoms E. Therefore, further investigation of the absorption rate should be performed. One kilogram of the fresh plant was dried under mild sunshine.
It is suggested that, this venom containing procoagulant factors with molecular weight of about 56 kDa. Generally envenoming by Echis snake vipers is responsible for several clinical complications of severe systemic and local pathology. Protein measurement with the Folin phenol reagent.
The peaks were monitored at nm All guinea pigs treated with venom E.