Russell S Viper Venom
Mostrando 1-6 de 6 artigos, teses e dissertações.
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1. Antibacterial potential of a basic phospholipase A2(VRV-PL-VIIIa) from Daboia russelii pulchella (Russell's viper) venom
Abstract Background: Microbial/bacterial resistance against antibiotics poses a serious threat to public health. Furthermore, the side effects of these antibiotics have stimulated tremendous interest in developing new molecules from diverse organisms as therapeutic agents. This study evaluates the antibacterial potential o
J. Venom. Anim. Toxins incl. Trop. Dis. Publicado em: 11/08/2015
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2. Novel role of antiplatelet agents (aspirin plus clopidogrel) in an incoagulable blood of a victim of russell's viper snakebite
Snake antivenom is a specific antidote to the venom action, neutralizing the circulating venom. However, it fails to neutralize the venom fixed to target organs such as platelets, renal tubules, etc. Russell's viper venom initiates rapid coagulation in a victim by activating blood platelets, factors V, X, and anticoagulant cofactors. Activation of thrombin,
Journal of Venomous Animals and Toxins including Tropical Diseases. Publicado em: 2006
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3. The Thromboplastic Activity of Russell's Viper Venom and Its Relationship to Factor VII
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4. In vivo externalization of phosphatidylserine and phosphatidylethanolamine in the membrane bilayer and hypercoagulability by the lipid peroxidation of erythrocytes in rats.
Phospholipid distribution across erythrocyte membrane bilayer is asymmetrical. In normal erythrocytes, entire phosphatidylserine (PS) and most of the phosphatidylethanolamine (PE) is present on the cytoplasmic side of membrane bilayer, whereas phosphatidylcholine (PC) and sphingomyelin (SM) are predominantly present at the outer side of membrane bilayer. The
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5. A factor X-activating cysteine protease from malignant tissue.
A proteolytic procoagulant has been identified in extracts of human and animal tumors and in cultured malignant cells. It directly activated Factor X but its similarity to other Factor S-activating serine proteases was not clear. This study describes work done to determine whether this enzyme, cancer procoagulant, is a serine or cysteine protease. Purified c
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6. Activation of human factor IX (Christmas factor).
Human Factor IX (Christmas factor) is a single-chain plasma glycoprotein (mol wt 57,000) that participates in the middle phase of the intrinsic pathway of blood coagulation. It is present in plasma as a zymogen and is converted to a serine protease, Factor IXabeta, by Factor XIa (activated plasma thromboplastin antecedent) in the presence of calcium ions. In