Results 161 to 170 of about 1,785 (202)
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Bothrops Moojeni Venom Peptides Containing Bradykinin Potentiating Peptides Sequences

Protein & Peptide Letters, 2001
Eight peptides were isolated from Bothrops moojeni venom by filtration followed by HPLC. MALDI mass spectroscopy and Edman degradation determined the purity, Mr and sequence of the peptides, respectively. Three (BmP7, BmP8 and BmvP11) of them were homologues with the biologically active B.
S. Bourguignon   +6 more
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Biochemical and biological differentiation of the venoms of the lancehead vipers (Bothrops atrox, Bothrops asper, Bothrops marajoensis and Bothrops moojeni)

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1992
Abstract 1. 1. Venoms of B. asper, B. atrox, B. marajoensis and B. moojeni collected in different regions were analyzed by their enzymatic activity and polyacrylamide gel electrophoreses (acidic, basic and SDS). 2. 2. These species can be recognized and distinguished by their characteristic protein electrophoretic patterns. 3. 3.
Marina T. Assakura   +2 more
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Renal toxicity of Bothrops moojeni snake venom and its main myotoxins

Toxicon, 2002
Acute renal failure is one the most common systemic complications after snakebite, however, its pathogenesis remains obscure. In this study we evaluated the renal effects of Bothrops moojeni venom and its myotoxins (Bmtx-I and BmtxII) in rat isolated perfused kidneys.
P S F, Barbosa   +9 more
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BthMP: a new weakly hemorrhagic metalloproteinase from Bothrops moojeni snake venom

Toxicon, 2009
In this work, a new weakly hemorrhagic metalloproteinase (BthMP) was purified from Bothrops moojeni snake venom. This enzyme was homogeneous by native and SDS-PAGE. It showed a polypeptide chain of 23.5kDa, pI=7.1, and N-terminal blocked. BthMP is comprised of high proteolytic activity on casein, fibrin and bovine fibrinogen, with no coagulating ...
Mário Sérgio R, Gomes   +9 more
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Ecology of the Pitviper, Bothrops moojeni, in the Brazilian Cerrado

Journal of Herpetology, 2003
Bothrops moojeni is a member of the atrox group that occurs in central and southeastern Brazil and adjacent Paraguay and Argentina. We describe habitat use, diel and seasonal activity, biometry, feeding habits, and reproduction of B. moojeni, based on field studies and analysis of 207 preserved specimens.
Cristiano Nogueira   +2 more
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Bothrops moojeni Hoge Moojen’s fer de lance, caicaca

1971
The karyotypes shown here were obtained from short term cultures of blood. The female is the heterogametic sex, the 4th pair of macrochromosomes correspond to the sex chromosomes ZW. Both specimens were captured in Sao Paulo, Brazil, and are preserved in the Collection of the Instituto Butantan.
Maria Luiza Beçak   +6 more
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Bothrops moojeni snake venom-induced renal glomeruli changes in rat.

The American journal of tropical medicine and hygiene, 2002
The venom of Bothrops moojeni has potent proteolytic and phospholipase A2 activities. In previous work, we showed that intravenous injection of this venom in rats decreased creatinine clearance and caused tubular dysfunction and histopathological changes with no alterations in blood pressure.
Patrícia Aline, Boer-Lima   +2 more
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Effects of photobiostimulation on edema and hemorrhage induced by Bothrops moojeni venom

Lasers in Medical Science, 2011
Antivenom (AV) treatment has been ineffective in neutralizing the severe local fast-developing tissue damage following snake-bite envenoming. We studied the effectiveness of low-level laser (LLL) and light-emitting diode (LED) irradiation alone or in combination with AV in reducing local edema formation and hemorrhage induced by Bothrops moojeni venom (
Nikele, Nadur-Andrade   +5 more
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Cytotoxic l-amino acid oxidase from Bothrops moojeni: Biochemical and functional characterization

International Journal of Biological Macromolecules, 2007
An L-amino acid oxidase isolated from Bothrops moojeni snake venom (BmooLAAO-I) was purified to a high degree using sequential CM-Sepharose ion-exchange and phenyl-Sepharose chromatography. When analyzed by mass spectrometry, the purified BmooLAAO-I presented a molecular weight of 64,889 and 130,779 under denaturing and nondenaturing conditions ...
Rodrigo G, Stábeli   +11 more
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Characterization Of A Hemagglutinating Glycoprotein Isolated From Bothrops Moojeni Snake Venom

Protein & Peptide Letters, 2001
From the crude snake venom of Bothrops moojeni, a homodimeric lectin was purified by affinity chromatography in lactose and was named BMooL. This lectin appeared to be a glycoprotein because it reacted with Schiffs reagent. The hemagglutinating activity of BMooL is inhibited by galactoside, EDTA, EGTA and DTT.
B. Kassab   +3 more
openaire   +1 more source

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