نتایج جستجو برای: anticoagulant factorchromatographyechis carinatussnake venom

تعداد نتایج: 22733  

2012
Toktam Mehdizadeh Kashani Hossein Vatanpour Hossein Zolfagharian Hasan Hooshdar Tehrani Mohammad Hossein Heydari Farzad Kobarfard

Platelet aggregation inhibitory effect and anticoagulant properties of fractions separated from the venoms of Cerastes persicus fieldi and Echis carinatus were investigated. The partial fractionation was performed on a Sephadex G-100 column. Two fractions separated from Cerastes persicus fieldi showed anti platelet aggregation activity on ADP (200 μM)-induced platelet aggregation (ca 80% inhibi...

2017
Thien Vu Tran Anh Ngoc Hoang Trang Thuy Thi Nguyen Trung Van Phung Khoa Cuu Nguyen Alexey V Osipov Igor A Ivanov Victor I Tsetlin Yuri N Utkin

Scorpion venoms are complex polypeptide mixtures, the ion channel blockers and antimicrobial peptides being the best studied components. The coagulopathic properties of scorpion venoms are poorly studied and the data about substances exhibiting these properties are very limited. During research on the Heterometrus laoticus scorpion venom, we have isolated low-molecular compounds with anticoagul...

Journal: :Journal of clinical pathology 1969
C D Forbes A G Turpie J C Ferguson G P McNicol A S Douglas

The action of the venom of the gaboon viper (Bitis gabonica) on blood coagulation, platelets, and the fibrinolytic enzyme system was studied. The results confirm that the venom of Bitis gabonica has a marked anticoagulant action in vitro. The venom appears to impair clot formation by a direct proteolytic action on fibrinogen, releasing soluble breakdown products.

Journal: :Journal of clinical pathology 1970
N MacKay J C Ferguson G P McNicol

The venom of the rhinoceros horned viper (Bitis nasicornis) has been studied in vitro and has been shown to be anticoagulant. This action appeared to be due to an effect on both the extrinsic and intrinsic blood thromboplastin mechanisms. The venom was also proteolytic and in purified caseinolytic systems activated plasminogen, enhanced the activation of plasminogen by streptokinase, and potent...

2014
Ashis K. Mukherjee Bhargab Kalita Rupamoni Thakur

BACKGROUND The monocled cobra (Naja kaouthia) is responsible for snakebite fatality in Indian subcontinent and in south-western China. Phospholipase A2 (PLA2; EC 3.1.1.4) is one of the toxic components of snake venom. The present study explores the mechanism and rationale(s) for the differences in anticoagulant potency of two acidic PLA2 isoenzymes, Nk-PLA2α (13463.91 Da) and Nk-PLA2β (13282.38...

1936
R. N. Chopra A. C. Roy

teristic pharmacological properties. With this end in view we started with cobra venom and Russell's viper venom. The cobra and Russell's viper belong to two different families of snakes, viz, Colubridce and Viperidce, respectively, and though the venoms from these have some characteristics in common they differ strikingly in other respects. For instance the neurotoxic element is preponderant i...

Journal: :Acta biochimica Polonica 2013
Mahdi Babaie Hossein Zolfagharian Hossein Salmanizadeh Abbas Zare Mirakabadi Hafezeh Alizadeh

Many snake venoms comprise different factors, which can either promote or inhibit the blood coagulation pathway. Coagulation disorders and hemorrhage belong to the most prominent features of bites of the many vipers. A number of these factors interact with components of the human blood coagulation. This study is focused on the effect of Echis carinatus snake venom on blood coagulation pathway. ...

Journal: :Thrombosis and haemostasis 2003
Ene Siigur Anu Aaspõllu Jüri Siigur

Amino acid sequences of two anticoagulant serine fibrinogenases - alpha- and beta-fibrinogenase (VLAF and VLBF) from Vipera lebetina venom have been deduced from the cDNA sequences encoding the enzymes. The mature protein sequences of 234 amino acids (VLAF) and 233 amino acids (VLBF) exhibit significant similarity with other snake venom serine proteinases. Both enzymes contain the catalytic tri...

Journal: :Toxicon : official journal of the International Society on Toxinology 2014
Ashis K Mukherjee Stephen P Mackessy

A 7.1 kDa basic peptide (Rusvikunin-II) was purified from a previously described protein complex (Rusvikunin complex, consists of Rusvikunin and Rusvikunin-II) of Daboia russelii russelii venom. The N-terminal sequence of Rusvikunin-II was found to be blocked, but peptide mass fingerprinting analysis indicated its identity as Kunitz-type basic protease inhibitor 2, previously reported from Russ...

2013
Elham Amrollahi Byoki Abbas Zare Mirakabadi

OBJECTIVE(S) Snake venoms contain complex mixture of proteins with biological activities. Some of these proteins affect blood coagulation and platelet function in different ways. Snake venom toxin may serve as a starting material for drug design to combat several pathophysiological problems such as cardiovascular disorders. In the present study, purification of anticoagulation factor from venom...

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