scholarly journals Bordonein-L, a new L-amino acid oxidase from Crotalus durissus terrificus snake venom: isolation, preliminary characterization and enzyme stability

2015 ◽  
Vol 21 (1) ◽  
Author(s):  
Karla C. F. Bordon ◽  
Gisele A. Wiezel ◽  
Hamilton Cabral ◽  
Eliane C. Arantes
Keyword(s):  
Amino Acid ◽  
Snake Venom ◽  
Enzyme Stability ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Crotalus Durissus Terrificus ◽  
Preliminary Characterization ◽  
Crotalus Durissus

Insights into the structure, function and stability of bordonein-L, the first L-amino acid oxidase from Crotalus durissus terrificus snake venom

Biochimie ◽  
2019 ◽  
Vol 163 ◽  
pp. 33-49 ◽  
Author(s):  
Gisele A. Wiezel ◽  
Joane K. Rustiguel ◽  
David Morgenstern ◽  
Karina F. Zoccal ◽  
Lucia H. Faccioli ◽  
...  
Keyword(s):  
Amino Acid ◽  
Structure Function ◽  
Snake Venom ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Crotalus Durissus Terrificus ◽  
Crotalus Durissus

Snake venom color and L-amino acid oxidase: An evidence of long-term captive Crotalus durissus terrificus venom plasticity

Toxicon ◽  
2021 ◽  
Vol 193 ◽  
pp. 73-83
Author(s):  
Eduardo Oliveira Venancio de Lima ◽  
Lídia Jorge Tasima ◽  
Daniela Miki Hatakeyama ◽  
Caroline Serino-Silva ◽  
Caroline Fabri Bittencourt Rodrigues ◽  
...  
Keyword(s):  
Amino Acid ◽  
Snake Venom ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Crotalus Durissus Terrificus ◽  
Crotalus Durissus

Isolation, characterization and screening of the in vitro cytotoxic activity of a novel L-amino acid oxidase (LAAOcdt) from Crotalus durissus terrificus venom on human cancer cell lines

Toxicon ◽  
2016 ◽  
Vol 119 ◽  
pp. 203-217 ◽  
Author(s):  
Tuila Leveghim Teixeira ◽  
Viviane Aline Oliveira Silva ◽  
Daniel Batista da Cunha ◽  
Flávia Lino Polettini ◽  
Camila Daniele Thomaz ◽  
...  
Keyword(s):  
Amino Acid ◽  
Cytotoxic Activity ◽  
Human Cancer ◽  
Acid Oxidase ◽  
Human Cancer Cell ◽  
Amino Acid Oxidase ◽  
Crotalus Durissus Terrificus ◽  
Human Cancer Cell Lines ◽  
Crotalus Durissus

Impairment of Platelet Aggregation by Echis colorata Venom Mediated by L-Amino Acid Oxidase or H2O2

1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne
Keyword(s):  
Hydrogen Peroxide ◽  
Amino Acid ◽  
Platelet Aggregation ◽  
Snake Venom ◽  
Oxidase Activity ◽  
Enzyme Preparation ◽  
Acid Oxidase ◽  
Crude Venom ◽  
Amino Acid Oxidase ◽  
Hemostatic Disorders

SummaryEchis colorata bites cause impairment of platelet aggregation and hemostatic disorders. The mechanism by which the snake venom inhibits platelet aggregation was studied. Upon fractionation, aggregation impairment activity and L-amino acid oxidase activity were similarly separated from the crude venom, unlike other venom enzymes. Preparations of L-amino acid oxidase from E.colorata and from Crotalus adamanteus replaced effectively the crude E.colorata venom in impairment of platelet aggregation. Furthermore, different treatments known to inhibit L-amino acid oxidase reduced in parallel the oxidase activity and the impairment potency of both the venom and the enzyme preparation. H2O2 mimicked characteristically the impairment effects of L-amino acid oxidase and the venom. Catalase completely abolished the impairment effects of the enzyme and the venom. It is concluded that hydrogen peroxide formed by the venom L-amino acid oxidase plays a role in affecting platelet aggregation and thus could contribute to the extended bleeding typical to persons bitten by E.colorata.

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