Results 161 to 170 of about 2,679 (199)
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Non-conventional toxins from Elapid venoms

Toxicon, 2003
Non-conventional toxins constitute a poorly characterized class of three-finger toxins isolated exclusively from Elapidae venoms. These toxins are monomers of 62-68 amino acid residues and contain five disulfide bridges. However, unlike alpha/kappa-neurotoxins and kappa-neurotoxins which have the fifth disulfide bridge in their middle loop (loop II ...
Nirthanan, S   +4 more
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Clinical Aspects of Elapid Bite

1971
Although the elapid family comprises numerous species, the rationale of dealing with the clinical aspects of their bites jointly is their having in common neurotoxic symptomatology as the preponderant feature. In this characteristic they differ from the Viperidae and the Crotalidae whose bites mainly produce blood clotting disturbances, hemorrhage, and
André de Vries, Eleanor Condrea
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Proteins toxic to arthropods in the venom of elapid snakes

Journal of Insect Physiology, 1975
It has been found that the lethal action of elapid snake venoms to arthropods (fly larvae and isopods) is due to proteic factors differing from the toxins which are strongly and specifically active on mammals. This conclusion was based on the following: (1) Lack of any correlation between the toxic activity on larvae, isopods, and mice of ten elapid
E, Zlotkin   +4 more
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Properties of some 3-nitrotyrosyl elapid venom cardiotoxins

International Journal of Biochemistry, 1987
Nitration of the invariant Tyr-22 in Hemachatus haemachates cardiotoxin 12B did not greatly decrease lethality, and the haemolytic potency towards guinea-pig erythrocytes remained unchanged. This residue is thus non-essential for cardiotoxin to exert its biological action.
F H, Carlsson, A I, Louw
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Paraspecific protection by elapid and sea snake antivenins

Toxicon, 1967
Abstract Seventeen elapid antivenins and one sea snake antivenin were tested for neutralizing activity against a panel of fifteen elapid venom samples (eight Naja, three Bungarus, one each of Ophiophagus, Hemachatus, Walterinnesia and Micrurus) and one sea snake (Enhydrina) sample. Assays were made by injecting mice subcutaneously with 2–10 ld 50 of
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A comparative study of the biological properties of Australian elapid venoms

Comparative Biochemistry and Physiology Part C: Comparative Pharmacology, 1990
1. The hemorrhagic, procoagulant, anticoagulant, protease, phosphodiesterase, alkaline phosphomonoesterase, L-amino acid oxidase, acetylcholinesterase, arginine ester hydrolase, phospholipase A, 5'-nucleotidase and hyaluronidase activities of 39 samples of venoms from 13 species (15 taxa) of Australian elapids were determined and the Sephadex G-75 gel ...
N H, Tan, G, Ponnudurai
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A comparative study of the homology of certain enzymes in elapid venoms

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1971
Abstract 1. 1. Similar electrophoretic mobilities for esterases with identical substrate specificities have been shown for the venoms of several closely related elapidae. 2. 2. Two lactate dehydrogenase isozymes were shown for most Naja venoms with the slower migrating band (at alkaline pH's) showing constant mobility for all Naja species
R L, McLean, E J, Massaro, W B, Elliott
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Further studies on the mass of venom injected by Elapid snakes

Toxicon, 1983
Further experimental studies to determine the mass of venom injected by medically-significant Australian elapids are reported. The use of a modified enzyme immunoassay technique to measure venom injected during snake bite is presented. The feeding biting pattern of the Australian eastern brown snake (Pseudonaja textilis) is described.
J J, Morrison   +3 more
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Behavioral Thermoregulation in Australian Elapid Snakes

Copeia, 1980
Behavioral thermoregulation in laboratory thermal gradients was studied in seven species of Australian snakes of the Elapidae: Acanthophis antarcticus, Austrelaps superbus, Notechis scutatus, Pseudechis porphyriacus, Pseudonaja nuchalis, P. textilis and Unechis flagellum.
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Structure and pharmacology of elapid cytotoxins

Pharmacology & Therapeutics, 1988
M J, Dufton, R C, Hider
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