Results 121 to 130 of about 112,374 (150)
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Molecular characterisation of endogenous snake venom metalloproteinase inhibitors

Biochemical and Biophysical Research Communications, 2008
Viper venoms contain one of the most potent mixtures of proteases in natural existence and yet the venom gland and proteins in this mixture are refractory to degradation. Here we demonstrate that the sub-10-kDa components of venom from two African viper species (Echis ocellatus and Cerastes cerastes cerastes) are predominantly composed of the tri ...
Wagstaff, Simon C.   +7 more
openaire   +4 more sources

Timeline of key events in snake venom metalloproteinase research

Journal of Proteomics, 2009
It is reasonable to state that snake venom toxinology has been actively pursued for at least the past 400 to 500 years. Early on it was appreciated that the venoms of the Viperidae produced profound local effects, notably hemorrhage. For the past 100 years, with the advent of modern chemistry and biochemistry significant progress has been gained ...
Jay W, Fox, Solange M T, Serrano
openaire   +2 more sources

On the ancestral recruitment of metalloproteinases into the venom of snakes

Toxicon, 2012
Tracing the evolutionary history of proteins can reveal insights into gene alterations responsible for changes in structure and function. Here, the origin of snake venom metalloproteinases was rigorously reassessed using phylogenetics and the reconstruction of ancestral sequences.
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Evidence for heterogeneous forms of the snake venom metalloproteinase jararhagin: a factor contributing to snake venom variability

Archives of Biochemistry and Biophysics, 2003
The reprolysin subfamily of metalloproteinases includes snake venom metalloproteinases (SVMP) and mammalian disintegrin/metalloproteinase. These proteins are synthesized as zymogens and undergo proteolytic processing resulting in a variety of multifunctional proteins. Jararhagin is a P-III SVMP isolated from the venom of Bothrops jararaca.
A M, Moura-da-Silva   +8 more
openaire   +2 more sources

Insights into the mechanism of haemorrhage caused by snake venom metalloproteinases

Toxicon, 1996
Local and systemic haemorrhage are common consequences of crotaline and viperine envenoming. Several studies carried out using purified toxins have indicated that local haemorrhage can be attributed to a distinct class of venom metalloproteinases. Analyses of their cDNAs predict multi-domain enzymes, with an N-terminal metalloproteinase domain, a ...
A S, Kamiguti   +3 more
openaire   +2 more sources

Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases

Toxicon, 2005
The importance of proteinases in the pathologies associated with Viperid envenoming has long been appreciated. Over the past 40 years substantial research has clearly implicated metalloproteinases in the venom (snake venom metalloproteinases; SVMPs) as playing key roles in the development of such symptoms as hemorrhage, edema, hypotension, hypovolemia,
Solange M T Serrano, Jay Fox
exaly   +3 more sources

Isolation and cloning of a metalloproteinase from king cobra snake venom

Toxicon, 2007
A 50 kDa fibrinogenolytic protease, ohagin, from the venom of Ophiophagus hannah was isolated by a combination of gel filtration, ion-exchange and heparin affinity chromatography. Ohagin specifically degraded the alpha-chain of human fibrinogen and the proteolytic activity was completely abolished by EDTA, but not by PMSF, suggesting it is a ...
Xiao-Xi, Guo   +4 more
openaire   +2 more sources

Doxycycline-Mediated Inhibition of Snake Venom Phospholipase and Metalloproteinase

Military Medicine
ABSTRACT Introduction Warfighters are exposed to life-threatening injuries daily and according to the Joint Trauma System Military Clinical Practice Guideline—Global Snake Envenomation Management snakebites are a concerning threat in all theaters of operation.
Daniel K Arens   +8 more
openaire   +2 more sources

A New Family of Proteinases is Defined by Several Snake Venom Metalloproteinases

Biological Chemistry Hoppe-Seyler, 1992
Recently, the complete amino acid sequences have been determined for several snake venom metalloproteinases from the genera Crotalus, Trimeresurus and Lachesis of the Crotalidae family. Among these are both hemorrhagic and nonhemorrhagic metalloproteinases.
L A, Hite, J W, Fox, J B, Bjarnason
openaire   +2 more sources

BJ46a, a snake venom metalloproteinase inhibitor

European Journal of Biochemistry, 2001
Fractionation of the serum of the venomous snake Bothrops jararaca with (NH4)2SO4, followed by phenyl‐Sepharose and C4‐reversed phase chromatographies, resulted in the isolation of the anti‐hemorrhagic factor BJ46a. BJ46a is a potent inhibitor of the SVMPs atrolysin C (class P‐I) and jararhagin (P‐III) proteolytic activities and B.
R H, Valente   +4 more
openaire   +2 more sources

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