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애플리케이션
Snake venom from Echis carinatus (Indian saw-scaled viper) which acts primarily on fibrinogen may be used as a source of anticoagulation factors and the prothrombin activator ecarin. It may also be used as an immunogen.
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Acute Tox. 2 Dermal - Acute Tox. 2 Oral
Storage Class Code
6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
John Kim et al.
Xenobiotica; the fate of foreign compounds in biological systems, 45(8), 663-671 (2015-02-13)
1. The safety, tolerability, pharmacokinetics, pharmacodynamics, and food effect of LB30870, a new selective thrombin inhibitor, were studied in 16 healthy men. 2. A double-blind, placebo-controlled single ascending dose study was done at oral doses of 5, 15, 30, 60, 120, and
Riley B Peacock et al.
Biochemistry, 57(18), 2694-2703 (2018-04-11)
Thrombin normally cleaves fibrinogen to promote coagulation; however, binding of thrombomodulin to thrombin switches the specificity of thrombin toward protein C, triggering the anticoagulation pathway. The W215A thrombin mutant was reported to have decreased activity toward fibrinogen without significant loss
Effects of snake venom proteases on human fibrinogen chains.
Cortelazzo A, Guerranti R, Bini L, et al.
Blood, 8, 120-125 (2010)
K Paul et al.
Toxicon : official journal of the International Society on Toxinology, 50(7), 893-900 (2007-08-08)
High titer antibodies (IgY) were raised in egg yolk of white leghorn chicken (Gallus gallus domesticus) by immunizing with the venom of Echis carinatus (Saw scaled viper or carpet viper), an Indian venomous snake belonging to the family Viperidae. The
Isolation and partial purification of anticoagulant fractions , from the venom of the Iranian snake Echis carinatus.
Babaie M, Zolfagharian H, et al.
Bioengineered (2012)
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