Enzyme Thrombin Like
Mostrando 13-24 de 34 artigos, teses e dissertações.
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13. Structural and functional characterisation of a serine proteinase TLBm, isolated starting from the Bothrops marajoensis whole venom / Caracterização estrutural e funcional de uma serinoprotease TLBm, isolada a partir do veneno total de Bothrops marajoensis
Muitas das toxinas isoladas e estudadas em seus efeitos biológicos precisam ser reavaliadas à luz de metodologias otimizadas em HPLC e confirmadas por espectrometria de massas, devido à possível presença de algum componente não estudado. No caso da serpente Bothrops marajoensis, são valorizados os estudos sobre essa espécie devido aos poucos trabalho
Publicado em: 2008
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14. Isolation and characterization of a serine proteinase with thrombin-like activity from the venom of the snake Bothrops asper
A serine proteinase with thrombin-like activity was isolated from the venom of the Central American pit viper Bothrops asper. Isolation was performed by a combination of affinity chromatography on aminobenzamidine-Sepharose and ion-exchange chromatography on DEAE-Sepharose. The enzyme accounts for approximately 0.13% of the venom dry weight and has a molecul
Brazilian Journal of Medical and Biological Research. Publicado em: 17/12/2007
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15. Caracterização cinética da protease trômbica presente no veneno de "Bothrops leucurus":: leucurobina.
It was obtained in this work more data about leucurobin, a snake venom thrombin-like enzyme from Bothrops leucurus, very common in Brazilian Northeast. The kinetic parameters KM, kcat, kcat/KM over p-nitroanilin chromogenic substrates was determined. The coagulant activity over citrated human plasma and purified bovine fibrinogen was evaluated. Leucurobin ha
Publicado em: 2006
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16. Micrurus spixii (PERUVIAN CORAL SNAKE) VENOM - PRELIMINARY BIOCHEMICAL AND ENZYMATIC CHARACTERIZATION
Micrurus spixii venom was studied after fractionation by Sephadex G-100 SF gel filtration chromatography. Several enzymatic activities and biological effects were investigated in whole venom and fractions. The venom was resolved in four peaks in a range of about 73.2-10.7 kDa molecular weight. Alkaline phosphatase and acetylcholinesterase activities were fou
Journal of Venomous Animals and Toxins. Publicado em: 2002
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17. Two related thrombin-like enzymes present in Bothrops atrox venom
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%
Brazilian Journal of Medical and Biological Research. Publicado em: 2000-11
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18. Mechanism of Action of Thrombin on Fibrinogen, I. Synthesis of Fibrinogen-like Peptides, and Their Proteolysis by Thrombin and Trypsin
In a study of the action of thrombin on fibrinogen and a comparison of this enzyme with trypsin, several fibrinogen-like oligopeptides were synthesized. The hydrolysis of the arginyl-glycine bond in these peptides, by both of these enzymes, is examined and compared.
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19. The complete nucleotide sequence of the gene for batroxobin, a thrombin-like snake venom enzyme.
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20. Endothelin-like pulmonary vasoconstrictor peptide release by alpha-thrombin.
The endothelial cells lining the vessel wall can modulate vasomotor tone by releasing vasoactive factors, such as endothelial-derived constricting factors. We observed that alpha-thrombin, but not catalytically inactivated alpha-thrombin, mediated the release of two pulmonary vasoconstrictor peptides into the venous effluent of guinea pig lungs. These peptid
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21. Enhancement of respiratory syncytial virus-induced cytopathology by trypsin, thrombin, and plasmin.
A series of proteases of diverse substrate specificity were tested for their effect on respiratory syncytial virus-induced cytopathology. Three of the enzymes, thrombin, plasmin, and trypsin, were able to augment significantly the fusion of virus-infected A549 cells. On a concentration basis, thrombin was the most active promoter, followed by plasmin and the
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22. Glu-192----Gln substitution in thrombin mimics the catalytic switch induced by thrombomodulin.
In serine proteases, residue 192, three residues prior to the active site Ser-195, plays an important role in determining substrate specificity. In trypsin (EC 3.4.21.4) and most trypsin-like enzymes with relatively broad specificity, this position is occupied by Gln. In thrombin (EC 3.4.21.5), an enzyme with restricted specificity, position 192 is occupied
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23. Kallikrein-like activity of crotalase, a snake venom enzyme that clots fibrinogen.
During the amino acid sequence determination of crotalase (EC 3.4.21.30), the thrombin-like enzyme from the venom of Crotalus adamanteus (eastern diamondback rattlesnake), we found that, in addition to the expected structural homology with bovine thrombin (EC 3.4.21.5), there was even greater homology with porcine pancreatic kallikrein (EC 3.4.21.8). In expl
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24. Differential proteolytic activation of factor VIII-von Willebrand factor complex by thrombin.
Blood coagulation factor VIII (fVIII) is a plasma protein that is decreased or absent in hemophilia A. It is isolated as a mixture of heterodimers that contain a variably sized heavy chain and a common light chain. Thrombin catalyzes the activation of fVIII in a reaction that is associated with cleavages in both types of chain. We isolated a serine protease