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Crotalus durissus ruruima

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https://www.readbyqxmd.com/read/25598498/neuromuscular-effects-of-venoms-and-crotoxin-like-proteins-from-crotalus-durissus-ruruima-and-crotalus-durissus-cumanensis
#1
COMPARATIVE STUDY
Walter Luís Garrido Cavalcante, Luis Alberto Ponce-Soto, Sérgio Marangoni, Márcia Gallacci
A myographic study was performed to compare the neuromuscular effects of venoms and crotoxin-like proteins from Crotalus durissus ruruima and Crotalus durissus cumanensis in mice phrenic-diaphragm preparation. It was concluded that both venoms present neurotoxic activity as a consequence of their crotoxin content. Furthermore, crotoxin from C.d. cumanensis is more potent than that from C.d. ruruima venom. At the concentration range in which both venoms express neurotoxic activity, only C.d. cumanensis venom also manifest a direct myotoxic effect that probably involves the synergic participation of other components than crotoxin...
March 2015: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/21130107/comparison-of-the-effect-of-crotalus-simus-and-crotalus-durissus-ruruima-venoms-on-the-equine-antibody-response-towards-bothrops-asper-venom-implications-for-the-production-of-polyspecific-snake-antivenoms
#2
COMPARATIVE STUDY
Maria Cristina Dos-Santos, Cynthia Arroyo, Sergio Solano, María Herrera, Mauren Villalta, Alvaro Segura, Ricardo Estrada, José María Gutiérrez, Guillermo León
Antivenoms are preparations of immunoglobulins purified from the plasma of animals immunized with snake venoms. Depending on the number of venoms used during the immunization, antivenoms can be monospecific (if venom from a single species is used) or polyspecific (if venoms from several species are used). In turn, polyspecific antivenoms can be prepared by purifying antibodies from the plasma of animals immunized with a mixture of venoms, or by mixing antibodies purified from the plasma of animals immunized separately with single venom...
February 2011: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/20223257/effect-of-the-synthetic-coumarin-ethyl-2-oxo-2h-chromene-3-carboxylate-on-activity-of-crotalus-durissus-ruruima-spla2-as-well-as-on-edema-and-platelet-aggregation-induced-by-this-factor
#3
F V Fonseca, L Baldissera, E A Camargo, E Antunes, E B S Diz-Filho, A G Corrêa, L O S Beriam, D O Toyama, C A Cotrim, Joel Alvin, M H Toyama
We show that ethyl 2-oxo-2H-chromene-3-carboxylate (EOCC), a synthetic coumarin, irreversibly inhibits phospholipase A(2) (sPLA2) from Crotalus durissus ruruima venom (sPLA2r) with an IC(50) of 3.1 +/- 0.06 nmol. EOCC strongly decreased the V(max) and K(m), and it virtually abolished the enzyme activity of sPLA2r as well as sPLA2s from other sources. The edema induced by sPLA2r + EOCC was less than that induced by sPLA2r treated with p-bromophenacyl bromide, which was more efficient at neutralizing the platelet aggregation activity of native sPLA2r...
July 2010: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/19863078/snake-venomics-of-the-central-american-rattlesnake-crotalus-simus-and-the-south-american-crotalus-durissus-complex-points-to-neurotoxicity-as-an-adaptive-paedomorphic-trend-along-crotalus-dispersal-in-south-america
#4
Juan J Calvete, Libia Sanz, Pedro Cid, Pilar de la Torre, Marietta Flores-Díaz, M Cristina Dos Santos, Adolfo Borges, Adolfo Bremo, Yamileth Angulo, Bruno Lomonte, Alberto Alape-Girón, José María Gutiérrez
We report a comparative venomic and antivenomic characterization of the venoms of newborn and adult specimens of the Central American rattlesnake, Crotalus simus, and of the subspecies cumanensis, durissus, ruruima, and terrificus of South American Crotalus durissus. Neonate and adult C. simus share about 50% of their venom proteome. The venom proteome of 6-week-old C. simus is predominantly made of the neurotoxic heterodimeric phospholipase A(2) (PLA(2) crotoxin) (55.9%) and serine proteinases (36%), whereas snake venom Zn(2+)-metalloproteinases (SVMPs), exclusively of class PIII, represent only 2% of the total venom proteins...
January 2010: Journal of Proteome Research
https://www.readbyqxmd.com/read/19673100/biochemical-and-biological-characterization-of-a-pla2-from-crotoxin-complex-of-crotalus-durissus-cumanensis
#5
Jaime Andrés Pereañez, Vitelbina Núñez, Salomón Huancahuire-Vega, Sergio Marangoni, Luis Alberto Ponce-Soto
A new PLA2 (Cdcum6) from crotoxin complex of Colombian Crotalus durissus cumanensis rattlesnake was purified using molecular exclusion chromatography and RP-HPLC. The molecular mass of Cdcum6 was determined by SDS-PAGE approximately 14 KDa and confirmed by MALDI-TOF (14321.98 Da). The enzyme showed Km 6.0 mM, Vmax 3.44 nmol/min, optimum pH was 8.0 and temperature was between 30 and 45 degrees C, and it had a strict requirement of Ca2+ for its activity. The N-terminal sequence of PLA2 was SLVQF EKMIK EVAGK NGVPWY...
April 2009: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/19470334/biochemical-and-biological-characterization-of-a-plar-2r-from-crotoxin-complex-of-crotalus-durissus-cumanensis
#6
Jaime Andrés Pereañez, Vitelbina Núñez, Salomón Huancahuire-Vega, Sergio Marangoni, Luis Alberto Ponce-Soto
A new PLAR(2) (Cdcum6) from crotoxin complex of Colombian Crotalus durissus cumanensis rattlesnake was purified using molecular exclusion chromatography and RP-HPLC. The molecular mass of Cdcum6 was determined by SDS-PAGE ~14 KDa and confirmed by MALDI-TOF (14321.98 Da). The enzyme showed Km 6.0mM, Vmax 3.44 nmol/min, optimum pH was 8.0 and temperature was between 30 - 45 degrees C and, and it had a strict requirement of CaP(2+P) for its activity. The N -- terminal sequence of PLAR(2R) was SLVQF EKMIK EVAGK NGVPWY...
January 30, 2009: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/19013478/enzymatic-and-structural-characterization-of-new-pla2-isoform-isolated-from-white-venom-of-crotalus-durissus-ruruima
#7
E B S Diz Filho, S Marangoni, D O Toyama, F H R Fagundes, S C B Oliveira, F V Fonseca, A K Calgarotto, P P Joazeiro, M H Toyama
This work reports the structural and enzymatic characterization of a new sPLA2 from the white venom of Crotalus durissus ruruima, nominated PLA2A. The homogeneity of the PLA2A fraction and its molecular mass were initially evaluated by SDS-PAGE and confirmed by MALDI-TOF spectrometry, indicating a molecular mass of 14,299.34Da. Structural investigation, through circular dichroism spectroscopy, revealed that PLA2A has a high content of alpha helix and beta-turn structures, 45.7% and 35.6% respectively. Its amino acid sequence, determined by Edman degradation and "de novo amino acid sequencing", exhibited high identity to PLA2 Cdt F15 from Crotalus durissus terrificus...
January 2009: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/17203396/biochemical-pharmacological-and-structural-characterization-of-two-pla2-isoforms-cdr-12-and-cdr-13-from-crotalus-durissus-ruruima-snake-venom
#8
Luis Alberto Ponce-Soto, Paulo Aparecido Baldasso, Frey Francisco Romero-Vargas, Flávia V Winck, José Camillo Novello, Sergio Marangoni
Cdr-12 and Cdr-13 isoforms of PLA2, a D49 protein, were purified from Crotalus durissus ruruima venom after one chromatographic step, reverse phase HPLC on micro-Bondapack C-18. The molecular mass by SDS-PAGE of Cdr-12 and Cdr-13 isoforms of PLA2 was 14333.49 Da and 14296.42 Da, respectively and confirmed by MALDI-TOF mass spectrometry. The amino acid composition showed that both isoforms Cdr-12 and Cdr-13 have a high content of Lys, Tyr, Gly, Arg, and 14 half-Cys residues, typical of a basic PLA2. The isoforms Cdr-12 and Cdr-13 had a sequence of amino acids of 122 amino acid residues, being Cdr-12: SLLQFNKMIK FETRKNAIPF YAFYGCYCGW GGQGRPKDAT DRCCIVHDCC YGKLAKCNTK WDFYRYSLRS GYFQCGKGTW CEQQICECDR VAAECLRRSL STYRYGYMIY PDSRCREPSE TC and pI value 8...
January 2007: Protein Journal
https://www.readbyqxmd.com/read/16269162/individual-venom-variability-in-crotalus-durissus-ruruima-snakes-a-subspecies-of-crotalus-durissus-from-the-amazonian-region
#9
COMPARATIVE STUDY
Maria Cristina Dos-Santos, Eduardo Borgesde Assis, Thémis Desiré Moreira, Janete Pinheiro, Consuelo Latorre Fortes-Dias
Venoms of six specimens of Crotalus durissus ruruima snakes from the same geographical site in the Brazilian State of Roraima, were individually assayed for their main pharmacological properties. Quantitative and qualitative differences were found and the presence of crotoxin-like isoforms in these venoms was indicated. Our findings corroborate the existence of a considerable intrapopulational variability in C. d. ruruima venoms, and the importance of using a pool of venoms for antivenom production, in general, in order to assure the neutralization of the maximum possible number of toxins from a given species...
December 15, 2005: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/15804530/specific-identification-of-lachesis-muta-muta-snake-venom-using-antibodies-against-the-plasminogen-activator-enzyme-lv-pa
#10
COMPARATIVE STUDY
Liza F Felicori, Carlos Chávez-Olórtegui, Eladio F Sánchez
Sandwich-type enzyme linked immunosorbent assays (ELISA) were developed to detect Lachesis muta muta (bushmaster) snake venom using antibodies against the plasminogen activator enzyme (LV-PA). Antibodies to LV-PA were obtained by immunization of one rabbit with the purified enzyme. The IgG fraction was purified from rabbit blood in a single step on a column of Sepharose-L. m. muta venom and used to coat the microtiter plates. The specificity of the assay was demonstrated by its capacity to correctly discriminate between the circulating antigens in mice that were experimentally inoculated with L...
May 2005: Toxicon: Official Journal of the International Society on Toxinology
https://www.readbyqxmd.com/read/8310446/-characterization-of-the-biological-activities-of-the-yellow-and-white-venoms-from-crotalus-durissus-ruruima-compared-with-the-crotalus-durissus-terrificus-venom-neutralizing-activity-of-crotalus-durissus-ruruima-antivenins
#11
M C Dos Santos, L C Ferreira, W D Da Silva, M F Furtado
The biological activities of 'yellow' and 'white' venom of a rattlesnake Crotalus durissus ruruima Hoge, 1965, found in the savanna-like vegetation (cerrado) of northern Brazil (Roraima) and Venezuela have been studied, and compared to the reference Crotalus durissus terrificus venom. The lethal activity of venoms depended on the inoculation route. The most toxic venom was the white one. The venoms of C. d. terrificus and the yellow of C. d. ruruima had similar lethalities. The yellow venom of C. d. ruruima showed a caseinolytic activity three times higher than that obtained with either the venom of C...
November 1993: Toxicon: Official Journal of the International Society on Toxinology
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