Results 151 to 160 of about 6,759 (190)

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, F. Paes, E. Calheiros, M. Juliano, A. Aguiar, A. Melgarejo, S. Giovanni-De-Simone   +6 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, D. de Carvalho, S. Marangoni, J. Novello   +3 more
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Cleavage of immunoglobulins by moojeni protease A, from the venom of Bothrops moojeni

Toxicon, 1990
Moojeni protease A, a proteolytic enzyme isolated from the venom of Bothrops moojeni hydrolyzes human and rabbit IgGs. The resulted fragments retained the combining though not the precipitating power or the property to fix complement. Similar to papain, moojeni protease A releases directly Fab fragments from IgG.
M T, Assakura, F R, Mandelbaum
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Proteolytic specificity of moojeni protease A isolated from the venom of Bothrops moojeni

Toxicon, 1993
Moojeni protease A, a proteolytic enzyme isolated from Bothrops moojeni venom, hydrolyzes type I collagen, gelatin, fibrinogen, fibrin and the B-chain of oxidized insulin. The proteinase cleaves the A alpha-chain faster than the B beta-chain of human fibrinogen and shows no effect on the gamma-chain.
A P, Reichl, F R, Mandelbaum
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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, Ana Maria, Barbosa, Fernando Pereira, Carlos, Carlos José, Lima, José Carlos, Cogo, Stella Regina, Zamuner   +5 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, Maria de Fatima Furtado, Fajga R. Mandelbaum   +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, A, Havt, P E G, Facó, T M, Sousa, I S A M, Bezerra, M C, Fonteles, M H, Toyama, S, Marangoni, J C, Novello, H S A, Monteiro   +9 more
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Isolation of the major proteolytic enzyme from the venom of the snake Bothrops moojeni (caissaca)

Toxicon, 1985
Moojeni protease A was purified from the venom of Bothrops moojeni by chromatography on Sephadex G-100, DEAE Sephadex A-50 and rechromatography on Sephadex G-100. The enzyme shows one protein band in polyacrylamide gel electrophoresis at pH 8.5 or at pH 4.3. The pI of moojeni protease A was approximately 7.7. In immunoelectrophoresis it migrates to the
M T, Assakura, A P, Reichl, M C, Asperti, F R, Mandelbaum   +3 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, Mirian M, Mendes, Fábio, de Oliveira, Rodrigo M, de Andrade, Carolina P, Bernardes, Amélia, Hamaguchi, Tânia M, de Alcântara, Andreimar M, Soares, Veridiana M, Rodrigues, Maria I, Homsi-Brandeburgo   +9 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, Willy Beçak, Franklin L. Roberts, Robert N. Shoffner, E. Peter Volpe, Kurt Benirschke, T. C. Hsu   +6 more
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