A new l -amino acid oxidase from Bothrops jararacussu snake venom: Isolation, partial characterization, and assessment of pro-apoptotic and antiprotozoal activities

2017 ◽  
Vol 103 ◽  
pp. 25-35 ◽  
Author(s):  
Sante E.I. Carone ◽  
Tássia R. Costa ◽  
Sandra M. Burin ◽  
Adélia C.O. Cintra ◽  
Karina F. Zoccal ◽  
...  
1982 ◽  
Vol 48 (03) ◽  
pp. 277-282 ◽  
Author(s):  
I Nathan ◽  
A Dvilansky ◽  
T Yirmiyahu ◽  
M Aharon ◽  
A Livne

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.


Biochimie ◽  
2019 ◽  
Vol 163 ◽  
pp. 33-49 ◽  
Author(s):  
Gisele A. Wiezel ◽  
Joane K. Rustiguel ◽  
David Morgenstern ◽  
Karina F. Zoccal ◽  
Lucia H. Faccioli ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document