Výsledky vyhledávání - "S. H. Andrião-Escarso"

Rabbit antivenom efficacy against myotoxic and neurotoxic activities of Bothrops jararacussu venom and bothropstoxin-I

Autor: Yoko Oshima-Franco, Stephen Hyslop, JoséR. Giglio, Maria Alice da Cruz-Höfling, S. H. Andrião-Escarso, Gildo Bernardo Leite, J. Prado-Franceschi, A. A. Valério, Léa Rodrigues-Simioni

Publikováno v: Journal of Venomous Animals and Toxins, Volume: 8, Issue: 2, Pages: 226-243, Published: 2002

Bothrops jararacussu venom and its major toxin bothropstoxin-I (BthTX-I) possess myotoxic and neurotoxic properties. The efficacy of a rabbit antivenom raised against B. jararacussu venom in the neutralization of physiological, biochemical, and morph

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b37a8c85f0a1bd65f1530eb654cbcca5
https://doi.org/10.1590/s0104-79302002000200004

Zobrazit plný text záznamu

Comparative Biochemical Studies of Myotoxic Phospholipase A2 From Bothrops Venom

Autor: M. R. M. Fontes, Marcos H. Toyama, José Roberto Giglio, A. M. Soares, Sergio Marangoni, B. Oliveira, S. H. Andrião-Escarso, J. C. Novello

Publikováno v: Protein & Peptide Letters. 8:179-186

Venoms from Bothrops jararcussu Bothrops asper Bothrops atrox Bothrops pirajai Bothrops moojeni Bothrops alternatus and Bothrops (Bothriopasis) bilineata were fractionated using a simplified procedure based on-exchange chromatography on CM-Sepharose

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6ba12ea43c7527da86277b0a2a4921c1
https://doi.org/10.2174/0929866013409445

Zobrazit plný text záznamu

A pH-Induced Dissociation of the Dimeric Form of a Lysine 49-Phospholipase A2Abolishes Ca2+-Independent Membrane Damaging Activity

Autor: José Roberto Giglio, A.H.C. de Oliveira, S. H. Andrião-Escarso, Richard J. Ward, and A. S. Ito

Publikováno v: Biochemistry. 40:6912-6920

The hydrolysis of phospholipids by class II phospholipase A2 (PLA2) involves a Ca2+ ion cofactor bound to the Asp49 residue in the active site region. In the lysine 49 phospholipase A2 homologues (Lys49-PLA2), the Asp49 residue is substituted by Lys,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42f8746d85c2659d33166a6d8e964715
https://doi.org/10.1021/bi0026728

Zobrazit plný text záznamu

Effects of aqueous extract of Casearia sylvestris (Flacourtiaceae) on actions of snake and bee venoms and on activity of phospholipases A2

Autor: Heyder da Silva Diniz, Márcia Helena Borges, Maria Inês Homsi-Brandeburgo, Sergio Lizano, Aristides Quintero, Veridiana M. Rodrigues, José María Gutiérrez, José Roberto Giglio, S. H. Andrião-Escarso, Amélia Hamaguchi, Andreimar M. Soares

Publikováno v: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 127:21-30

The crude aqueous extract from the leaves of Casearia sylvestris, a plant found in Brazilian open pastures, was assayed for its ability to inhibit phospholipase A2 (PLA2) activity and some biological activities of bee and several snake venoms, and of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a6588b6527bc3b1dfb1f5a29673775dc
https://doi.org/10.1016/s0305-0491(00)00237-6

Zobrazit plný text záznamu

The analgesic activity of crotamine, a neurotoxin from Crotalus durissus terrificus (South American rattlesnake) venom: A biochemical and pharmacological study

Autor: Adriana Cristina Mancin, José Roberto Giglio, S. H. Andrião-Escarso, Vitor M. Faça, Lewis J. Greene, Irene Rosemir Pelá, Sérgio Zuccolotto, Andreimar M. Soares

Publikováno v: Toxicon. 36:1927-1937

Crotamine, a 4.88 kDa neurotoxic protein, has been purified to apparent homogeneity from Crotalus durissus terrificus venom by gel filtration on Sephadex G-75. When injected (i.p. or s.c.) in adult male Swiss mice (20–25 g), it induced a time-dose

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46d28b6728b32f4a2b3b32f34597fddf
https://doi.org/10.1016/s0041-0101(98)00117-2

Zobrazit plný text záznamu

Inhibition of proteases, myotoxins and phospholipases A2 from Bothrops venoms by the heteromeric protein complex of Didelphis albiventris opossum serum

Autor: A. M. Soares, Márcia Helena Borges, Maria Inês Homsi-Brandeburgo, JoséR. Giglio, Veridiana M. Rodrigues, S. H. Andrião-Escarso, O.A.B. Cunha

Publikováno v: IUBMB Life. 43:1091-1099

The antibothropic complex (ABC) from opossum (species Didelphis albiventris) serum was purified by chromatography on DEAE-Sephacel. It showed an acidic character and two polypeptide chains of ca. 45 kDa and 48 kDa, respectively. Lyophilized opossum s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0f7f4adab4ce6b5a52e2a71656699d1
https://doi.org/10.1080/15216549700204911

Zobrazit plný text záznamu

Alkylation of myotoxic phospholipases A2 in Bothrops moojeni venom: a promising approach to an enhanced antivenom production

Autor: Silvana Marcussi, Rodrigo G. Stábeli, Carlos Alberto Vieira, Andreimar M. Soares, José Roberto Giglio, Wladimir P. Sestito, O.A.B. Cunha, S. H. Andrião-Escarso

Publikováno v: The international journal of biochemistrycell biology. 36(2)

Bothrops moojeni crude venom (MjCV) and its two major toxins, namely myotoxin I (MjTX-I) and myotoxin II (MjTX-II) were alkylated by p-bromophenacyl bromide (BPB). After alkylation the i.p. LD(50) (mice) of MjCV and MjTX-I/II increased from 6.0 to 15

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a786e269c85e0939ae7d38058338be2c
https://pubmed.ncbi.nlm.nih.gov/14643891

Zobrazit plný text záznamu

Structural and functional characterization of an acidic platelet aggregation inhibitor and hypotensive phospholipase A(2) from Bothrops jararacussu snake venom

Autor: Fernando M.A. Correa, Lewis J. Greene, André Lopes Fuly, José César Rosa, José Roberto Giglio, S. H. Andrião-Escarso, Marcos R.M. Fontes, Andreimar M. Soares

Publikováno v: Biochemical pharmacology. 64(4)

An acidic (pI approximately 4.5) phospholipase A(2) (BthA-I-PLA(2)) was isolated from Bothrops jararacussu snake venom by ion-exchange chromatography on a CM-Sepharose column followed by reverse phase chromatography on an RP-HPLC C-18 column. It is a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b72a1377c42375bf535374906ba30493
https://pubmed.ncbi.nlm.nih.gov/12167491

Zobrazit plný text záznamu

Pathological alterations induced by neuwiedase, a metalloproteinase isolated from Bothrops neuwiedi snake venom

Autor: José Roberto Giglio, Aida Franceschi, José María Gutiérrez, S. H. Andrião-Escarso, Alexandra Rucavado, Andreimar M. Soares, Veridiana M. Rodrigues

Publikováno v: Biochimie; Volumen 83, Número 6. 2001
Kérwá
Universidad de Costa Rica
instacron:UCR

The pathological alterations induced by neuwiedase, a 22 kDa class P-I metalloproteinase from the venom of the South American pit viper Bothrops neuwiedi, were studied in mice. Neuwiedase was devoid of hemorrhagic activity when tested in the skin up

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b1f7ac5f0d151f2dfeed83fefbf8d88
http://www.sciencedirect.com/science/article/pii/S0300908401012822

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání