Results 131 to 140 of about 7,766 (180)

L-amino acid oxidase from Bothrops atrox snake venom triggers autophagy, apoptosis and necrosis in normal human keratinocytes. [PDF]

Sci Rep, 2019
Costal-Oliveira F, Stransky S, Guerra-Duarte C, Naves de Souza DL, Vivas-Ruiz DE, Yarlequé A, Sanchez EF, Chávez-Olórtegui C, Braga VMM.   +8 more
europepmc   +1 more source

Snakebite Envenomations In The Brazilian Amazon: A Little Less Neglected. [PDF]

Rev Soc Bras Med Trop
Sachett J, Wen FH, Costa AGD, Murta F, Carvalho ES, Araújo FQ, Machado VA, Silva Neto AVD, Bisneto PF, Val F, Ferreira LCL, Figueira E, Sartim MA, Monteiro W.   +13 more
europepmc   +1 more source

<i>Bothrops</i> venom variation drives niche-specific pharmacology through Ca²⁺ signalling and membrane damage. [PDF]

Front Pharmacol
Bourke LA, Slagboom J, Waller MA, Neely GG, Kool J, Cardoso FC.   +5 more
europepmc   +1 more source

Antimicrobial peptidomes of Bothrops atrox and Bothrops jararacussu snake venoms [PDF]

Amino Acids, 2021
The worrisome emergence of pathogens resistant to conventional drugs has stimulated the search for new classes of antimicrobial and antiparasitic agents from natural sources. Antimicrobial peptides (AMPs), acting through mechanisms that do not rely on the interaction with a specific receptor, provide new possibilities for the development of drugs ...
Saulo Luis da Silva, Cleopatra Alves Da Silva Caldeira, Daniel C Pimenta   +2 more
exaly   +5 more sources

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Coagulant and esterase activities of thrombin and Bothrops atrox venom

Toxicon, 1972
Abstract Thrombin and Bothrops atrox coagulant are similar enzyme proteins. Contrary to the general contention, TAME hydrolyzing enzyme was found by the authors to differ from the coagulant component of both the thrombin preparation and the B. atrox venom. With the thrombin preparation and B. atrox venom, the hydrolysis of synthetic amino acid esters
A, Devi, S, Banerjee, A L, Copley
openaire   +3 more sources

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
openaire   +1 more source

Properties of nerve growth factor from the venom of Bothrops atrox

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
A glycoprotein fraction islated in poor yield (approx. 0.04%) from the venom of Bothrops atrox contained nerve growth factor. The material had biological activity, stability, the property of anomalous adsorption onto surfaces, apparent molecular weight and sub-unit structure that were similar to those for nerve growth factor that had been previously ...
R E, Glass, D V, Banthorpe
openaire   +2 more sources

Purification and characterization of phosphodiesterase I from Bothrops atrox

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1976
Phosphodiesterase I from the venom of Bothrops atrox has been purified by successive chromatography on phosphocellulose P-11, hydroxyapatite, and DEAE-cellulose DE 52. The final product gave a single band on sodium dodecylsulfate-polyacrylamide gels and was free of endonuclease, 5' -nucleotidase, and unspecific alkaline phosphatase activity.
openaire   +2 more sources

Purification of a Phosphodiesterase from Bothrops atrox Venom by Affinity Chromatography

European Journal of Biochemistry, 1973
The purification of a phosphodiesterase from Bothrops atrox venom by chromatography on phosphocellulose and affinity chromatography with O‐(4‐nitrophenyl)‐O′‐phenyl‐thiophosphate ester coupled to activated Sepharose is described. Phosphatases are removed by chromatography on hydroxyapatite.
A M, Frischauf, F, Eckstein
openaire   +2 more sources