Results 111 to 120 of about 1,391 (163)

Venomics across the <i>Bothrops neuwiedi</i> Species Complex Revealed a P-III Snake Venom Metalloproteases/K49-PLA<sub>2</sub> Dichotomy and a Remarkable Paraspecific Neutralization of the Brazilian Pentabothropic Antivenom. [PDF]

open access: yesJ Proteome Res
Galizio NDC   +15 more
europepmc   +1 more source
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Circulating vasotocin in the snake Bothrops jararaca

Comparative Biochemistry and Physiology Part A: Physiology, 1992
1. There is biochemical and pharmacological evidence to suggest the presence of vasotocin in the blood and plasma of the snake Bothrops jararaca (Bj). 2. XE-64 extracts from Bj blood showed antidiuretic and hypotensive activities in rats and a contractile effect on rat isolated uterus, which was totally dialysable and inhibited by thioglycollate.
P F, Silveira   +3 more
openaire   +2 more sources

Purification of a proteinase inhibitor from the plasma of Bothrops jararaca (jararaca)

Toxicon, 1991
A proteinase inhibitor was isolated from the plasma of Bothrops jararaca by three chromatographic steps: DEAE Sephacel, Phenyl Sepharose and Bio Gel P200. It inhibited caseinolytic and hemorrhagic activity of the whole venom of B. jararaca. Proteolytic activity of bothropasin and J protease, both metalloproteinases of the venom, were neutralized by the
M M, Tanizaki   +3 more
openaire   +2 more sources

The vasopressor action of angiotensin in the snake Bothrops jararaca

Comparative Biochemistry and Physiology Part A: Physiology, 1992
1. Carotid blood pressure from anesthetized B. jararaca snakes was recorded in order to study angiotensin action in this reptile. 2. Whereas [Asn1,Val5] AII and AIII were less potent than [Asp1,Ile5] AII and [Asp1,Val5] AII, [Sar1,Ile5] AII was slightly more potent. 3. Captopril abolished the responses to AI (0.01-3 micrograms/kg). 4.
M C, Breno, Z P, Picarelli
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Distinct bothrojaracin isoforms produced by individual jararaca (Bothrops jararaca) snakes

Toxicon, 1997
Bothrojaracin (apparent mol. wt 27,000) is a potent inhibitor of thrombin previously isolated from the venom of Bothrops jararaca. Several molecular variants (isoforms) have been identified in a pool of venom collected from a large number of animals. In order to determine whether an individual snake produces a single type of bothrojaracin or multiple ...
R Q, Monteiro   +4 more
openaire   +2 more sources

Bothrops jararaca Wied

1971
The karyotypes presented were obtained from short term blood cultures. The sex chromosomes, male — ZZ, female — ZW correspond to the 4th pair of macrochromosomes. The karyotypes are from a male specimen of Santa Catarina and from a female specimen of Sao Paulo, Brazil. Both are preserved in the Collection of the Instituto Butantan.
Maria Luiza Beçak   +6 more
openaire   +1 more source

Immunization with liposome-encapsulated Bothrops jararaca venom

Toxicon, 2000
The venom of Bothrops jararaca (BjV) snake was encapsulated into liposomes. The toxicity and ability of the resultant liposomes to protect mice were evaluated. No acute toxicity was found in mice, when liposomes were subcutaneously injected whereas the same dose of venom emulsified in Freund's adjuvant caused the mice to die.
V T, Carvalho   +3 more
openaire   +2 more sources

The humoral immune responses of patients bitten by the snake Bothrops jararaca (jararaca)

Toxicon, 1990
The isotype and specificity of antibodies produced by patients bitten by B. jararaca and submitted to serum therapy were studied. The IgG anti-B. jararaca antibodies have large individual dispersion, starting to appear 10 days after the first bite and increasing to at least 80 days after the bite.
M O, Domingos   +3 more
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Blood-clotting Activity of the Venom of Bothrops jararaca

Nature, 1959
THE well-known blood-clotting activity of the venom from snakes of various species of the genus Bothrops has been attributed to its proteolytic activity1, although Michl2 (using paper electrophoresis) and Holz and Raudonat3 (using fractional precipitation with ammonium sulphate) have presented evidence against this point of view.
O B, HENRIQUES   +2 more
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Angiotensin receptor in the heart of Bothrops jararaca snake

European Journal of Pharmacology, 2001
Angiotensin II interacts with specific cell surface angiotensin AT1 and AT2 receptors and, in some vertebrates, with an atypical angiotensin AT receptor. This study was designed to characterize the angiotensin receptor in the heart of Bothrops jararaca snake.
M C, Breno, C S, Porto, Z P, Picarelli
openaire   +2 more sources

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