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| Soares,A. M.; Oliveira,C. Z.; Santana,C. D.; Menaldo,D. L.; Silveira,L. B.; Teixeira,S. S.; Rueda,A. Q.; Marcussi,S.. |
| This work succinctly describes the professional and scientific life of Dr. José R. Giglio, one of the most outstanding Brazilian researchers in the field of Toxinology. During his long and successful career, he has made major contributions, especially in elucidating the function, structure, and mechanisms of action of animal venom proteins (from snakes, scorpions and spiders) as well as the characterization of antibodies and several inhibitors of venoms and toxins. We present here a brief history of Dr. Giglios personal and professional life, also reporting some of his numerous published scientific articles on venoms from snakes (Bothrops, Crotalus, and other genera), scorpions (Tityus sp), spiders (Phoneutria sp), their isolated toxins and natural... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Toxinology; Animal venoms; Toxins; Inhibitors; Homage; Giglio JR. |
| Ano: 2007 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400003 |
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| Costa,J. O.; Petric,C. B.; Hamaguchi,A.; Homsi-Brandeburgo,M. I.; Oliveira,C. Z.; Soares,A. M.; Oliveira,F.. |
| Two fibrinogenolytic enzymes, Bothrops alternatus metalloprotease isoform (BaltMP)-I and II, were purified from Bothrops alternatus venom using Diethylaminoethyl (DEAE) Sephacel, Sephadex G-75 and Heparin-Agarose column chromatography. Purified BaltMP-I and II ran as single protein bands on analytical polyacrylamide gel electrophoresis and showed molecular weights of 29000 and 36000, respectively, under reducing conditions in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). BaltMP-II, but not BaltMP-I, displayed blood-clotting activity in bovine plasma, which was about 10-fold higher than that of the crude venom. Both enzymes were proteolytically active against bovine fibrinogen as substrate. When fibrinogen and each enzyme were... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Snake venom; Bothrops alternatus; Metalloproteases; Functional characterization; Fibrinogenolytic activity; Defibrinogenation in vivo. |
| Ano: 2007 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000300007 |
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| Borja-Oliveira,C. R.; Kassab,B. H.; Soares,A. M.; Toyama,M. H.; Giglio,J. R.; Marangoni,S.; Re,L.; Rodrigues-Simioni,L.. |
| Two presynaptic phospholipases A2 (PLA2), neuwieditoxin-I (NeuTX-I) and neuwieditoxin-II (NeuTX-II), were isolated from the venom of Bothrops neuwiedi pauloensis (BNP). The venom was fractionated using molecular exclusion HPLC (Protein-Pak 300SW column), followed by reverse phase HPLC (µBondapak C18 column). Tricine-SDS-PAGE in the presence or absence of dithiothreitol showed that NeuTX-I and NeuTX-II had a molecular mass of approximately 14 kDa and 28kDa, respectively. At 10µg/ml, both toxins produced complete neuromuscular blockade in indirectly stimulated chick biventer cervicis isolated preparation without inhibiting the response to acetylcholine, but NeuTX-II reduced the response to KCl by 67.0±8.0% (n=3; p<0.05). NeuTX-I and NeuTX-II are probably... |
| Tipo: Info:eu-repo/semantics/article |
Palavras-chave: Chick biventer cervicis; Loose patch clamp; Nerve-muscle preparation; Neuromuscular junction; Neurotoxicity; PLA2 neurotoxin; Presynaptic action; Bothrops neuwiedi pauloensis; Neuwieditoxin-I; Neuwieditoxin-II. |
| Ano: 2007 |
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000100008 |
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