A single-base-pair substitution abolishes d-amino-acid oxidase activity in the mouse

Author(s):  
Masato Sasaki ◽  
Ryuichi Konno ◽  
Masahiro Nihio ◽  
Akira Niwa ◽  
Yosihiro Yasumura ◽  
...  
FEBS Letters ◽  
2004 ◽  
Vol 563 (1-3) ◽  
pp. 55-58 ◽  
Author(s):  
Katsumi Omagari ◽  
Hidehisa Yoshimura ◽  
Mitsunori Takano ◽  
Dongyun Hao ◽  
Masayuki Ohmori ◽  
...  

1994 ◽  
Vol 4 (3) ◽  
pp. 227-228 ◽  
Author(s):  
John W. Pierpont ◽  
Luke D. Doolan ◽  
Kurt Amann ◽  
Greg R. Snead ◽  
Robert P. Erickson

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.


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