scholarly journals Role of l-amino acid oxidase isolated from Calloselasma rhodostoma venom on neutrophil NADPH oxidase complex activation

Toxicon ◽  
2018 ◽  
Vol 145 ◽  
pp. 48-55 ◽  
Author(s):  
Mauro Valentino Paloschi ◽  
Charles Nunes Boeno ◽  
Jéssica Amaral Lopes ◽  
André Eduardo dos Santos da Rosa ◽  
Weverson Luciano Pires ◽  
...  
1993 ◽  
Vol 268 (36) ◽  
pp. 26941-26949
Author(s):  
A D'Aniello ◽  
G D'Onofrio ◽  
M Pischetola ◽  
G D'Aniello ◽  
A Vetere ◽  
...  

2010 ◽  
Vol 107 (26) ◽  
pp. E107-E107 ◽  
Author(s):  
S. Millecamps ◽  
S. Da Barroca ◽  
C. Cazeneuve ◽  
F. Salachas ◽  
P.-F. Pradat ◽  
...  

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.


In haemolysates of non-nucleated erythrocytes there is an inverse proportion between catalase activity and rate of choleglobin formation on addition of ascorbic acid. In the intact erythrocytes catalase protects haemoglobin against oxidation and further destruction by the hydrogen peroxide generated by the D-amino-acid oxidase system or by physiological concentrations of ascorbic acid and glutathione. Acid destromatization of haemolyzed horse erythrocytes causes a small decrease in the catalase activity and an increased rate of inactivation of the remaining catalase by ascorbic acid. The liberation of copper from haemocuprein is quantitatively insufficient to explain the decreased stability of the catalase. Exposing duck oxyhaemoglobin, but not reduced haemoglobin, to a pH of 5⋅5 to 5⋅8, causes an alteration which is apparent from the increase of the rate of choleglobin formation. The mechanism of this alteration is discussed. It partly explains the 'stroma effect', at least in duck erythrocytes. In addition, in the latter, there is a true stroma effect. Choleglobin formation in the presence of ascorbic acid is accelerated by a variety of substances. Some of these perturb haemoglobin, while others increase the formation of hydrogen peroxide from ascorbic acid. The implications of our findings on the mechanism of choleglobin formation and on the role of catalase in the erythrocyte are discussed.


2001 ◽  
Vol 268 (14) ◽  
pp. 4044-4053 ◽  
Author(s):  
Armin Geyer ◽  
Teresa B. Fitzpatrick ◽  
Peter D. Pawelek ◽  
Karina Kitzing ◽  
Alice Vrielink ◽  
...  

Author(s):  
Nazanin R. Kondori ◽  
Praveen Paul ◽  
Jacqueline P. Robbins ◽  
Ke Liu ◽  
John C. W. Hildyard ◽  
...  

2016 ◽  
Vol 38 (2) ◽  
pp. 128-134 ◽  
Author(s):  
Cristiane Tavares ◽  
Thaís Maciel ◽  
Sandra Burin ◽  
Luciana Ambrósio ◽  
Sandro Ghisla ◽  
...  

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Mauro Valentino Paloschi ◽  
Jéssica Amaral Lopes ◽  
Charles Nunes Boeno ◽  
Milena Daniela Souza Silva ◽  
Jaína Rodrigues Evangelista ◽  
...  

2010 ◽  
Vol 7 (6) ◽  
pp. 1413-1423 ◽  
Author(s):  
Yan-Fei Xin ◽  
Xin Li ◽  
Bin Hao ◽  
Nian Gong ◽  
Wen-Qiang Sun ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document