Proteolytic specificity of hemorrhagic toxin b from Crotalus atrox (western diamondback rattlesnake) venom.

@article{Hagihara1985ProteolyticSO,
  title={Proteolytic specificity of hemorrhagic toxin b from Crotalus atrox (western diamondback rattlesnake) venom.},
  author={Shigeru Hagihara and Yumiko Komori and Anthony T. Tu},
  journal={Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology},
  year={1985},
  volume={82 1},
  pages={
          21-7
        }
}
  • S. Hagihara, Y. Komori, A. Tu
  • Published 1985
  • Biology, Chemistry
  • Comparative biochemistry and physiology. C, Comparative pharmacology and toxicology
10 Citations
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Proteolytic specificity, using oxidized insulin B chain, is similar to that of several hemorrhagic toxins found within the same venom, yet atroxase shows no hemorrhagic activity and exhibits low lethality when tested on Swiss Webster mice.
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The first report of the sequence of a direct‐acting, non‐hemorrhagic fibrinolytic enzyme found in snake venom, fibrolase, has been determined and reveals the absence of asparagine‐linked glycosylation sites defined by the consensus sequence.
Proteolytic, hemorrhagic and hemolytic activities of snake venoms.
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  • 2004
TLDR
Fibroblasts in culture under such conditions appear to mobilize glycogen, phosphocreatine, and protein for ATP production to compensate for decreased glucose.
The Effect of Walterinnesia aegyptia Venom Proteins on TCA Cycle Activity and Mitochondrial NAD+-Redox State in Cultured Human Fibroblasts
TLDR
Results indicate that the effects of venom proteins could be directed at the mitochondrial level and/or the rates of NAD(+) and NADP(+) biosynthesis.
Ophidian envenomation strategies and the role of purines.
  • S. Aird
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    Toxicon : official journal of the International Society on Toxinology
  • 2002

References

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Proteolytic specificity of hemorrhage toxin a isolated from western diamondback rattlesnake (Crotalus atrox) venom.
TLDR
The proteolytic specificity of hemorrhagic toxin a from the venom of Crotalus atrox (western diamondback rattlesnake) has been investigated by using the oxidized B chain of bovine insulin and other peptides as substrates, and the absence of hydrolytic activity against the last two substrates indicates that hemorrhagic toxins a does not possess trypsin- or chymotrypsins-like activity.
Hemorrhagic toxins from Western diamondback rattlesnake (Crotalus atrox) venom: isolation and characterization of five toxins and the role of zinc in hemorrhagic toxin e.
TLDR
Five previously unknown hemorrhagic proteins, designated hemorrhagic toxins a,b,c,d, and e, were isolated from the venom of the western diamondback rattlesnake and were demonstrated to be proteolytic when dimethylcasein and dimethylhemoglobin were used as substrates.
Isolation and characterization of a hemorrhagic proteinase from timber rattlesnake venom.
TLDR
A protein isolated from timber rattlesnake venom is hemorrhage inducing and lethal to mice and in conjunction with the loss of proteinase activity is a corresponding loss of lethal and hemorrhagic activities, suggesting that all three are related.
Presence of zinc in proteolytic hemorrhagic toxin isolated from Agkistrodon acutus venom.
The substrate specificity of thermomycolase, an extracellular serine proteinase from the thermophilic fungus Malbranchea pulchella var. sulfurea.
TLDR
The specificity of thermomycolase toward glucagon and the oxidized A and B chains of insulin was investigated, but ready hydrolysis of peptide bonds occurred within sequences containing non-polar residues, suggesting this endoproteinase must possess an extended hydrophobic binding site for polypeptides.
The specificity of purified porcine pancreatic elastase.
An electrophoretically homogeneous elastase preparation free from tryptic and chymotryptic activities was obtained by chromatography on DEAE-Sephadex and CM-cellulose. This preparation exhibits a
A Collagenolytic Enzyme from Aspergillus oryzae
TLDR
On the basis of the various types of proteolytic specificity found for the protease a new concept is put forward for understanding collagen breakdown in vivo and in vitro.
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