Isolation and characterization of an apoptotic and platelet aggregation inhibiting l-amino acid oxidase from Vipera berus berus (common viper) venom

2006 ◽  
Vol 1764 (4) ◽  
pp. 707-714 ◽  
Author(s):  
Mari Samel ◽  
Heiki Vija ◽  
Gunilla Rönnholm ◽  
Jüri Siigur ◽  
Nisse Kalkkinen ◽  
...  
Keyword(s):  
Amino Acid ◽  
Platelet Aggregation ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Vipera Berus ◽  
Isolation And Characterization

Isolation and characterization of a mitochondrial D-amino acid oxidase from Neurospora crassa

1977 ◽  
Vol 55 (1) ◽  
pp. 66-74 ◽  
Author(s):  
Melvin G. Rosenfeld ◽  
Edward H. Leiter
Keyword(s):  
Amino Acid ◽  
Neurospora Crassa ◽  
Mitochondrial Fraction ◽  
Acid Oxidation ◽  
Gel Chromatography ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Ph Optimum ◽  
Isolation And Characterization

D-Amino acid oxidase (EC 1.4.3.3) activity in homogenates of Neurospora crassa strain SY7A was found to sediment with the mitochondrial fraction. Digitonin fractionation studies on purified mitochondria have indicated a matrix localization of the enzyme. Additionally, a peroxidase (EC 1.11.1.7) activity, which may remove hydrogen peroxide formed as a product of D-amino acid oxidation, was also found in the mitochondrial matrix.Partial purification (20- to 30-fold) of the mitochondrial D-amino acid oxidase was achieved. The enzyme exhibited a pH optimum between 9.0 and 9.2, temperature optimum between 20 and 30 °C, and a molecular weight of 118 000 ± 6000 as determined by gel electrophoresis and 125 000 as determined by gel chromatography.

scholarly journals Isolation and Characterization of an L-Amino Acid Oxidase-Producing Marine Bacterium

Engineering ◽  
2013 ◽  
Vol 05 (10) ◽  
pp. 376-380 ◽  
Author(s):  
Zhiliang Yu ◽  
Hua Qiao ◽  
Juanping Qiu ◽  
Peiya Xu ◽  
Peng Li
Keyword(s):  
Amino Acid ◽  
Marine Bacterium ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Isolation And Characterization

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.

Comparative Characterization of Three D-Aspartate Oxidases and One D-Amino Acid Oxidase from Caenorhabditis elegans

2010 ◽  
Vol 7 (6) ◽  
pp. 1424-1434 ◽  
Author(s):  
Masumi Katane ◽  
Yasuaki Saitoh ◽  
Yousuke Seida ◽  
Masae Sekine ◽  
Takemitsu Furuchi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Caenorhabditis Elegans ◽  
Acid Oxidase ◽  
Amino Acid Oxidase ◽  
Comparative Characterization
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