scholarly journals Study on active response of superoxide dismutase and relevant binding interaction with bioaccumulated phthalates and key metabolites in Eisenia fetida

2021 ◽  
Vol 223 ◽  
pp. 112559
Author(s):  
Xiuli Fan ◽  
Chenggang Gu ◽  
Jun Cai ◽  
Yongrong Bian ◽  
Xinglun Yang ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Eisenia Fetida ◽  
Binding Interaction ◽  
Active Response

Characterization of an iron-containing superoxide dismutase from a higher plant, Citrus limonum

1994 ◽  
Vol 90 (2) ◽  
pp. 339-347 ◽  
Author(s):  
Maria S. Almansa ◽  
Luis A. del Rio ◽  
Francisca Sevilla
Keyword(s):  
Superoxide Dismutase ◽  
Higher Plant ◽  
Citrus Limonum

Superoxide, Xanthine Oxidase and Platelet Reactions: Further Studies on Mechanisms by which Oxidants Influence Platelets

1981 ◽  
Vol 45 (03) ◽  
pp. 290-293 ◽  
Author(s):  
Peter H Levine ◽  
Danielle G Sladdin ◽  
Norman I Krinsky
Keyword(s):  
Superoxide Dismutase ◽  
Cytochrome C ◽  
Xanthine Oxidase ◽  
Direct Effect ◽  
Platelet Function ◽  
Experimental Conditions ◽  
Release Reaction

SummaryIn the course of studying the effects on platelets of the oxidant species superoxide (O- 2), Of was generated by the interaction of xanthine oxidase plus xanthine. Surprisingly, gel-filtered platelets, when exposed to xanthine oxidase in the absence of xanthine substrate, were found to generate superoxide (O- 2), as determined by the reduction of added cytochrome c and by the inhibition of this reduction in the presence of superoxide dismutase.In addition to generating Of, the xanthine oxidase-treated platelets display both aggregation and evidence of the release reaction. This xanthine oxidase induced aggreagtion is not inhibited by the addition of either superoxide dismutase or cytochrome c, suggesting that it is due to either a further metabolite of O- 2, or that O- 2 itself exerts no important direct effect on platelet function under these experimental conditions. The ability of Of to modulate platelet reactions in vivo or in vitro remains in doubt, and xanthine oxidase is an unsuitable source of O- 2 in platelet studies because of its own effects on platelets.

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