1976
DOI: 10.1016/0005-2795(76)90249-x
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Purification and characterization of a coagulant protein from the venom of russell's viper

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1977
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Cited by 25 publications
(9 citation statements)
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“…Mercury (0.1 mM) had little or no effect on the procoagulant activity of Russell's viper venom, which is consistent with the observations of others (38); and 1 mM iodoacetamide seemed to stimulate the activity of Russell's viper venom. Thus, there was a clear distinction between the effect of these inhibitors on the activity of cancer procoagulant and the serine protease in Russell's viper venom.…”
Section: Introductionsupporting
confidence: 89%
See 1 more Smart Citation
“…Mercury (0.1 mM) had little or no effect on the procoagulant activity of Russell's viper venom, which is consistent with the observations of others (38); and 1 mM iodoacetamide seemed to stimulate the activity of Russell's viper venom. Thus, there was a clear distinction between the effect of these inhibitors on the activity of cancer procoagulant and the serine protease in Russell's viper venom.…”
Section: Introductionsupporting
confidence: 89%
“…Russell's viper venom standard was used to compare the effect of these inhibitors on a serine protease that activates Factor X in a well-characterized manner (27,(36)(37)(38). Mercury (0.1 mM) had little or no effect on the procoagulant activity of Russell's viper venom, which is consistent with the observations of others (38); and 1 mM iodoacetamide seemed to stimulate the activity of Russell's viper venom.…”
Section: Introductionsupporting
confidence: 76%
“…A fully lethal RV bite results in injection of 40–45 μg/mL of RVV in an adult human’s blood . WI RVV at all the tested doses exhibited pro-coagulant activity in in vitro conditions (Table and Figure ), attributed to the predominance of pro-coagulant SVMPs and SVSPs (Table and Figure ) in its venom. ,,,, Notably, high-molecular-mass pro-coagulant enzymes (>30 kDa) were separated in GF-1 to GF-4 fractions (Figure A and Table ), which corroborates well with the previous reports. ,,,, Nevertheless, WI RVV proteins in the mass range of 27–6 kDa (GF-5 to GF-8 gel filtration fractions) (Figure B) showed anti-coagulant activity (Table ). The above proteins are mostly PLA 2 s, KSPIs, and disintegrins (Table ), and their anti-coagulant action via enzymatic and/or non-enzymatic mechanism(s) has already been demonstrated. ,,,,,, Despite containing a higher proportion of anti-coagulant proteins (GF-5 to GF-8) compared to pro-coagulant proteins (GF-1 to GF-4) in WI RVV (Table a), in in vitro conditions crude RVV demonstrated pro-coagulant activity because pro-coagulant potency of the high-molecular-weight proteins surpasses the anti-coagulant activity of low-molecular-weight proteins (Table ).…”
Section: Resultsmentioning
confidence: 94%
“…18,20,21,33,56 Notably, high-molecular-mass pro-coagulant enzymes (>30 kDa) were separated in GF-1 to GF-4 fractions (Figure 3A and Table 3), which corroborates well with the previous reports. 20,21,56,69,70 Nevertheless, WI RVV proteins in the mass range of 27−6 kDa (GF-5 to GF-8 gel filtration fractions) (Figure 3B) showed anticoagulant activity (Table 3). The above proteins are mostly PLA 2 s, KSPIs, and disintegrins (Table 2), and their anticoagulant action via enzymatic and/or non-enzymatic mechanism(s) has already been demonstrated.…”
Section: Non-enzymatic Proteins Of Rvvmentioning
confidence: 99%
“…Once factor Xa is formed by either pathway, it can bind factor Va, phospholipid and calcium to form the prothrombinase complex that converts prothrombin to thrombin, which in turn clots fibrinogen 1. Factor X is one of the five vitamin K‐dependent blood coagulation proteins, the others being prothrombin, factor VII, factor IX and protein C. Factor X is a glycoprotein with a pivotal role in blood coagulation, and can be activated by intrinsic and extrinsic activating complexes, trypsin and certain snake venom 2–5…”
Section: Introductionmentioning
confidence: 99%