Results 131 to 140 of about 1,310 (165)
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Crotalid Snake Venom Subproteomes Unraveled by the Antiophidic Protein DM43

Journal of Proteome Research, 2009
Snake venoms are mixtures of proteins and peptides with different biological activities, many of which are very toxic. Several animals, including the opossum Didelphis aurita, are resistant to snake venoms due to the presence of neutralizing factors in their blood. An antihemorrhagic protein named DM43 was isolated from opossum serum. It inhibits snake
Surza L G, Rocha   +7 more
openaire   +2 more sources

Effects of Crotalid Venom on North American Snakes

Copeia, 1942
A LTHOUGH the question of the susceptibility of snakes to their own venom, or to venom of other species, has been of interest for some time, relatively little experimental work has been undertaken in this field. Most reports in the literature cite examples in which one snake was seen to bite another.
Hugh L. Keegan, Ted F. Andrews
openaire   +1 more source

Ophthalmic Exposure to Crotalid Venom

The Journal of Emergency Medicine, 2009
Crotalid venom exposure to the eye is uncommon. A 40-year-old woman sustained an accidental mucus membrane exposure of rattlesnake venom to her face and right eye. She was successfully treated with irrigation, topical antibiotics, and intravenous crotalid antivenin.
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California ground squirrel (Spermophilus beecheyi) blood sera inhibits crotalid venom proteolytic activity

Toxicon, 2000
Some California ground squirrels (Spermophilus beecheyi) show limited necrosis following envenomation by northern Pacific rattlesnakes (Crotalus viridis oreganus). This study demonstrates that S. beecheyi blood sera inhibits venom proteases. Sera from rattlesnake-abundant habitats inhibited C. v.
J E, Biardi, R G, Coss, D G, Smith
openaire   +2 more sources

Crotalid venom vascular endothelial growth factors has preferential affinity for VEGFR-1

Thrombosis and Haemostasis, 2005
SummaryPm-VEGF, a novel member ofVEGF family from the venom gland of Taiwan habu (Protobothrops mucrosquamatu), is a disulfidelinked homodimer with 119 amino acid residues. Recombinant fusion Pm-VEGF was expressed in Escherichia coli, purified and refolded.
Yuh-Ling, Chen   +3 more
openaire   +2 more sources

Surgical technique for isolation of the main venom gland of viperid, crotalid and elapid snakes

Toxicon, 1973
Abstract The main venom glands of venomous snakes were isolated in situ by a harmless surgical technique. The surgery had no apparent effect on the snakes' appearance, disposition or feeding habits more than 2 years after surgery. The snake, after surgery, could serve as an excellent preparation for studying the venom secretory process in the main ...
J L, Glenn, R, Straight, C C, Snyder
openaire   +3 more sources

Enzyme-linked immunosorbant assay (ELISA) of size-selected crotalid venom antigens by Wyeth's polyvalent antivenom

Toxicon, 1988
The binding of Antivenom (Crotalidae) Polyvalent to fractions from crude venoms of eight crotalid and one viperid snake, obtained by high performance size-exclusion chromatography, was determined with an indirect enzyme-linked immunosorbent assay (ELISA). Most of the large (greater than 30,000 mol.
R C, Schaeffer   +3 more
openaire   +2 more sources

The Clinical Problem of Crotalid Snake Venom Poisoning

1979
Bites by snakes of the family Crotalidae are usually medical emergencies requiring immediate attention and the exercise of considerable judgment. Delayed or inadequate treatment may result in undue harm to the patient and may result in tragic consequences.
openaire   +1 more source

The Mechanism of Snake Venom Actions—Rattlesnakes and Other Crotalids

1971
Of the nearly 2000 different types of snakes that exist, about 300 are known to be venomous. The venomous snakes are classified according to morphological characteristics and comprise five families: Crotalidae (crotalid), Viperidae (viperid), Elapidae (elapid), Hydrophiidae (sea-snakes), and Colubridae (colubrid).
openaire   +1 more source

A rapid method for the purification of monomeric and/or dimeric phospholipases A2 in crotalid snake venoms

Toxicon, 1985
We have developed a simple two-step procedure for the separation of monomeric (14,000 mol. wt) and dimeric (28,000 mol. wt) phospholipases A2 from the venoms of Crotalidae family snakes. All venom phospholipases A2 studied thus far exist as monomers under acidic conditions and are chromatographed as such on a column of G-50 Sephadex (superfine ...
W, Welches   +3 more
openaire   +2 more sources

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