Results 251 to 260 of about 64,120 (294)
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Hemorrhagic, myonecrotic, thrombotic and proteolytic activities of viper venoms.

Toxicon, 1969
Abstract Histolysis, thrombosis and proteolysis produced by venoms of vipers (Viperidae) from Asia, Europe and Africa were investigated. Some venoms showed hemorrhagic effects but not myonecrotic activity. Only Russell's viper from Thailand caused thrombosis. Four substrates were used to test for proteolytic activity of snake venoms.
A. Tu, M. Homma, B. Hong
semanticscholar   +4 more sources

Viper venom for control of postextraction hemorrhage

Oral Surgery, Oral Medicine, Oral Pathology, 1958
Abstract Viper venom is an effective hemostatic agent that converts prothrombin to thrombin in the presence of calcium. When applied to Oxycel gauze and placed in the socket of a recently extracted tooth, it will solve the vast majority of prolonged bleeding problems encountered in the practice of oral surgery.
William A. Wagner, Adrian O. Hubbell
openaire   +3 more sources

To Normalize or Not? Dilute Russell Viper Venom Time testing

American Journal of Clinical Pathology, 2022
Abstract Introduction/Objective Background: Antiphospholipid antibodies bind phospholipid bound proteins. Criteria for diagnosis of the antiphospholipid syndrome includes detection of either a lupus anticoagulant (LA) or anticardiolipin/anti B2GP1 antibodies and thrombotic events or pregnancy loss ...
Yong, Zhang   +2 more
openaire   +2 more sources

Heterogeneity of Russell's viper venom affects the sensitivity of the dilute Russell's viper venom time to lupus anticoagulants

Blood Coagulation & Fibrinolysis, 2004
A number of studies have shown that commercial dilute Russell's viper venom time (DRVVT) reagents vary in their sensitivity for lupus anticoagulant (LA) detection. The differences in performance are considered to be predominantly due to antibody heterogeneity and a wide variation in phospholipid content, and also the techniques and clot detection ...
Moore, G W, Savidge, G F
openaire   +3 more sources

Studies on venom and venom apparatus of Fea's viper, Azemiops feae

Toxicon, 1994
Enzyme activities tested in the venom gland extract of Azemiops feae snake are similar to those of viperine venoms, except that Azemiops venom has no blood clotting, haemorrhagic or myolytic activities. The venom gland exhibits the characteristic feature of a viperine gland, but the fangs possess a ridge at the tip laterally to the venom orifice and a ...
J. Meier, Dietrich Mebs, Ulrich Kuch
openaire   +2 more sources

Snake Venoms in Diagnostic Hemostasis and Thrombosis

Seminars in Thrombosis and Hemostasis, 2021
Snake venoms have evolved primarily to immobilize and kill prey, and consequently, they contain some of the most potent natural toxins. Part of that armory is a range of hemotoxic components that affect every area of hemostasis, which we have harnessed ...
G. W. Moore
semanticscholar   +1 more source

Inhibition of hemorrhagic activity of viper venoms by N-acetyl cysteine: involvement of N-acetyl and thiol groups.

Current Topics in Medicinal Chemistry, 2011
The mortality rate due to snakebite is reduced markedly by the use of anti-venoms, which are the only medically approved remedial agents available. The anti-venoms effectively neutralize the systemic toxicity but offer no protection towards local tissue ...
K. Sunitha   +5 more
semanticscholar   +1 more source

NORADRENALINE TRIGGERS VIPER'S VENOM

Journal of Experimental Biology, 2004
![][1] Most vipers don't waste their venom on any old mouthful. It takes time and energy to produce a gland-full of venom, so profligacy isn't an option. But just what triggers toxin synthesis wasn't clear until Norma Yamanouye and her colleagues began testing the response ...
openaire   +2 more sources

The complex toxic components of the Russell's viper venom

Biochemical and Biophysical Research Communications, 1976
Abstract Russell's viper venom has been fractionated on CM-cellulose, CM-Sephadex and Sephadex gel filtration and disc electrophoresis to obtain 4 toxins one of which is a glycoprotein with 2 subunits, one with 4 cationic subunits one of the subunits being dialysable, one with 3 cationic subunits and a dialysable low molecular weight minor toxin. The
Harish V. Bolar, Ravidatt W.P. Master
openaire   +3 more sources

[16] Coagulant protein of Russell's viper venom

1976
Publisher Summary Historically, the venom coagulant protein has been important in the elucidation of the activation mechanism of blood coagulation. In efforts to develop a therapy for the clotting defect in hemophilia, R. G. Macfarlane examined a number of snake venoms for their ability to accelerate blood coagulation.
Bruce Furie, Barbara C. Furie
openaire   +3 more sources

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