Consulta: subjectFacets:"Venoms"
Registros recuperados: 8
Data/hora: 13/06/2024 01:36:39

In vitro assay of biological and chemical toxins using antibodies against lethal toxin neutralizing factor
Provedor de dados: 79
Autores: LIPPS,B. V.
Lethal Toxin Neutralizing Factor (N-LTNF), MW 63.0 kDa, was isolated from opossum serum. After trypsin digestion, the active domain of N-LTNF was isolated and sequenced. The synthetic peptide consisting of ten amino acids was designated as LT-10. N-LTNF and LT-10 inhibited the lethality of animal, plant and bacteria toxins when tested on mice non-immunologically. The antibodies against N-LTNF and LT-10 only reacted immunologically with toxins and not with non-toxic substances. Anti-LTNF and anti-LT-10 reacted immunologically by ELISA test with toxins that were not detected by mouse test, such as cholera toxin and digoxin. Anti-LTNF and anti-LT-10 failed to react immunologically with non-toxic substances, such as nerve growth factor and collagen. Currently,...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Antibodies; In vitro assay; Lethal toxin neutralizing factor; Toxins; Venoms.
Ano: 2002
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302002000200003

Antileishmanial and antitrypanosomal activity of the cutaneous secretion of Siphonops annulatus
Provedor de dados: 80
Autores: Pinto,Erika Gracielle; Antoniazzi,Marta Maria; Jared,Carlos; Tempone,and Andre Gustavo.
Background Among the tropical parasitic diseases, those caused by protozoans are considered a challenge to public health, being represented by leishmaniasis and Chagas disease. In view of the low effectiveness and toxicity of the current therapy, animal venoms such as amphibian secretions have been used as a promising source of new drug prototypes. The present work aimed to achieve bioguided fractionation of metabolites present in a cutaneous secretion of the caecilian Siphonops annulatus (Amphibia: Gymnophiona: Siphonopidae) with antileishmanial and antitrypanosomal activity.Methods Through liquid-liquid partition and chromatographic techniques, the secretion was fractionated using bioguided assays. The 50% inhibitory concentration (IC50) of the main...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Amphibians; Venoms; Leishmania; Trypanosoma cruzi; Therapy; Drugs.
Ano: 2014
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992014000200340

Infiltrated plaques resulting from an injury caused by the common octopus (Octopus vulgaris): a case report
Provedor de dados: 80
Autores: Haddad Jr,Vidal; Magalhães,Claudia Alves de.
Several species of octopus are considered venomous due to toxins present in the glands connected to their “beak”, which may be associated with hunt and kill of prey. Herein, we report an accident involving a common octopus (Octopus vulgaris) that injured an instructor during a practical biology lesson and provoked an inflamed infiltrated plaque on the hand of the victim. The lesion was present for about three weeks and was treated with cold compresses and anti-inflammatory drugs. It was healed ten days after leaving a hyperchromic macule at the bite site. The probable cause of the severe inflammation was the digestive enzymes of the glands and not the neurotoxins of the venom.
Tipo: Info:eu-repo/semantics/report
Palavras-chave: Octopuses; Venomous animals; Aquatic animals; Venoms; Poisoning; Digestive enzymes.
Ano: 2014
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992014000200508

Mad, bad and dangerous to know: the biochemistry, ecology and evolution of slow loris venom
Provedor de dados: 80
Autores: Nekaris,K Anne-Isola; Moore,Richard S; Rode,E Johanna; Fry,Bryan G.
Only seven types of mammals are known to be venomous, including slow lorises (Nycticebus spp.). Despite the evolutionary significance of this unique adaptation amongst Nycticebus, the structure and function of slow loris venom is only just beginning to be understood. Here we review what is known about the chemical structure of slow loris venom. Research on a handful of captive samples from three of eight slow loris species reveals that the protein within slow loris venom resembles the disulphide-bridged heterodimeric structure of Fel-d1, more commonly known as cat allergen. In a comparison of N. pygmaeus and N. coucang, 212 and 68 compounds were found, respectively. Venom is activated by combining the oil from the brachial arm gland with saliva, and can...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Venoms; Ecology; Primates; Intraspecific competition; Predation; Ectoparasite; Naja naja.
Ano: 2013
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992013000100203

A C-type lectin from Bothrops jararacussu venom can adhere to extracellular matrix proteins and induce the rolling of leukocytes
Provedor de dados: 80
Autores: Elífio-Esposito,S. L.; Hess,P. L.; Moreno,A. N.; Lopes-Ferreira,M.; Ricart,C. A. O.; Souza,M. V.; Hasselman-Zielinski,F.; Becker,J. A.; Pereira,L. F.
Purification of a lectin from Bothrops jararacussu venom (BjcuL) was carried out using agarose-D-galactose affinity gel. MALDI-TOF gave a major signal at m/z 32028, suggesting the presence of a dimmer composed of two identical subunits. Divalent cations were required for the lectin activity, as complete absence of such ions reduced hemagglutination. BjcuL was more effective at neutral pH and showed total loss of activity at pH values below 4.0 and above 9.0. Its agglutinating activity remained stable at 25°C until 60min, but increased when at 35°C for at least 15min. Adhesion assays to extracellular matrix (ECM) glycoproteins showed that the biotinylated lectin (0.039-5.0µg/100µl) was capable of binding to fibronectin and vitronectin in a dose-dependent...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Venoms; Fibronectins; Vitronectin; Snakes; Intravital microscopy; Leukocytes.
Ano: 2007
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992007000400009

Hemolytic activity of venom from crown-of-thorns starfish Acanthaster planci spines
Provedor de dados: 80
Autores: Lee,Chi-Chiu; Tsai,Wann-Sheng; Hsieh,Hernyi Justin; Hwang,Deng-Fwu.
Background : The crown-of-thorns starfish Acanthaster planci is a venomous species from Taiwan whose venom provokes strong hemolytic activity. To understand the hemolytic properties of A. planci venom, samples were collected from A. planci spines in the Penghu Islands, dialyzed with distilled water, and lyophilized into A. planci spine venom (ASV) powder. Results : Both crude venom and ASV cause 50% hemolysis at a concentration of 20 μg/mL. The highest hemolytic activity of ASV was measured at pH 7.0-7.4; ASV-dependent hemolysis was sharply reduced when the pH was lower than 3 or greater than 8. There was almost no hemolytic activity when the Cu2+ concentration was increased to 10 mM. Furthermore, incubation at 100°C for 30 to 60 minutes sharply decreased...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Crown-of-thorns starfish; Spine; Venoms; Hemolysis.
Ano: 2013
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992013000100312

A new scenario of bioprospecting of Hymenoptera venoms through proteomic approach
Provedor de dados: 80
Autores: Santos,LD; Pieroni,M; Menegasso,ARS; Pinto,JRAS; Palma,MS.
Venoms represent a huge and essentially unexplored reservoir of bioactive components that may cure diseases that do not respond to currently available therapies. This review select advances reported in the literature from 2000 to the present about the new scenario of Hymenoptera venom composition. On account of new technologies in the proteomic approach, which presents high resolution and sensitivity, the combination of developments in new instruments, fragmentation methods, strategic analysis, and mass spectrometry have become indispensable tools for interrogation of protein expression, molecule interaction, and post- translational modifications. Thus, the biochemical characterization of Hymenoptera venom has become a major subject of research in the area...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Hymenoptera; Venoms; Allergens; Phospholipase A1; Wasp venom antigen 5; Hyaluronoglucosaminidase; Mass spectrometry; Proteomics.
Ano: 2011
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000400003

Two related thrombin-like enzymes present in Bothrops atrox venom
Provedor de dados: 56
Autores: Petretski,J.H.; Kanashiro,M.; Silva,C.P.; Alves,E.W.; Kipnis,T.L.
This article describes the presence of two new forms of a thrombin-like enzyme, both with apparent molecular masses of 38 kDa, in Bothrops atrox venom. Both share the ability to cleave fibrinogen into fibrin and to digest casein. Both present identical Km on the substrate BApNA. Their N-terminal amino acid sequences are identical for 26 residues, sharing 80% homology with batroxobin and flavoxobin. Two groups of monoclonal antibodies (mAbs) raised against the purified enzyme forms recognized different epitopes of the putative corresponding enzymes present in B. atrox crude venom. On Western blotting analysis of B. atrox crude venom, mAbs 5DB2C8, 5AA10 and 5CF11, but not mAbs 6CC5 and 6AD2-G5, revealed two or more protein bands ranging from 25 to 38 kDa. By...
Tipo: Info:eu-repo/semantics/article
Palavras-chave: Venoms; Bothrops atrox; Enzymes; Thrombin-like enzymes; Blood coagulation system.
Ano: 2000
URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000001100005