Behavioral characterization of a mutant mouse strain lacking d-amino acid oxidase activity

2011 ◽  
Vol 217 (1) ◽  
pp. 81-87 ◽  
Author(s):  
Min Zhang ◽  
Michael E. Ballard ◽  
Ana M. Basso ◽  
Natalie Bratcher ◽  
Kaitlin E. Browman ◽  
...  
1990 ◽  
Vol 46 (5) ◽  
pp. 468-470 ◽  
Author(s):  
H. Nagasaki ◽  
R. Yamada ◽  
R. Konno ◽  
Y. Yasumura ◽  
A. Iwashima

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.


Science ◽  
1943 ◽  
Vol 98 (2534) ◽  
pp. 89-89
Author(s):  
L. C. Clark ◽  
C. D. Kochakian ◽  
R. Phyllis Fox

2010 ◽  
Vol 7 (6) ◽  
pp. 1424-1434 ◽  
Author(s):  
Masumi Katane ◽  
Yasuaki Saitoh ◽  
Yousuke Seida ◽  
Masae Sekine ◽  
Takemitsu Furuchi ◽  
...  

1991 ◽  
Vol 23 (11) ◽  
pp. 1301-1305 ◽  
Author(s):  
Konno Ryuichi ◽  
Yamamoto Katsuhiko ◽  
Niwa Akira ◽  
Yasumura Yosihiro

2013 ◽  
Vol 41 (6) ◽  
pp. 1551-1556 ◽  
Author(s):  
Silvia Sacchi

Over the years, accumulating evidence has indicated that D-serine represents the main endogenous ligand of NMDA (N-methyl-D-aspartate) receptors. In the brain, the concentration of D-serine stored in cells is defined by the activity of two enzymes: serine racemase (responsible for both the synthesis and degradation) and D-amino acid oxidase (which catalyses D-serine degradation). The present review is focused on human D-amino acid oxidase, discussing the mechanisms involved in modulating enzyme activity and stability, with the aim to substantiate the pivotal role of D-amino acid oxidase in brain D-serine metabolism.


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