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Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom.
Cytotoxicity and inhibition of platelet aggregation caused by an l-amino acid oxidase from Bothrops leucurus venom.
Snake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: Contributing to its taxonomy and snakebite…
Biological activities of venoms from South American snakes.
Antigenic, microbicidal and antiparasitic properties of an l-amino acid oxidase isolated from Bothrops jararaca snake venom.
Pharmacological characterization and neutralization of the venoms used in the production of Bothropic antivenom in Brazil.
The novel metalloproteinase atroxlysin-I from Peruvian Bothrops atrox (Jergón) snake venom acts both on blood vessel ECM and platelets.
Venomic analysis and evaluation of antivenom cross-reactivity of South American Micrurus species.
Structural and functional characterization of a P-III metalloproteinase, leucurolysin-B, from Bothrops leucurus venom.
Isolation of a proteinase with plasminogen-activating activity from Lachesis muta muta (bushmaster) snake venom.
- E. Sanchez, C. I. Santos, M. Richardson
- Biology, ChemistryArchives of biochemistry and biophysics
- 1 June 2000
LV-PA exhibits a high degree of sequence identity with the TsVPA from Trimeresurus stejnegeri and with the Haly-PA from Agkistrodon halys and has homology with other snake venom serine proteinases such as the thrombin-like/gyroxin analogue from bushmaster venom and with other coagulation serine proteases.