Kinetic study of redox reaction of U(IV) with ferricyanide ions

1972 ◽  
Vol 37 (3) ◽  
pp. 762-767 ◽  
Author(s):  
Ľ. Adamčíková ◽  
Ľ. Treindl
Keyword(s):  
RSC Advances ◽  
2018 ◽  
Vol 8 (51) ◽  
pp. 29356-29367
Author(s):  
María Florencia Mangiameli ◽  
Sebastián Bellú ◽  
Bárbara Pérez Mora ◽  
Luis Sala ◽  
Nadia Mamana

The redox reaction between an excess of quinic acid (QA) and CrVI involves the formation of intermediates, namely, CrIV and CrV species, which in turn react with the organic substrates.


2008 ◽  
Vol 105 (12) ◽  
pp. 601-608
Author(s):  
Seung Min Han ◽  
Dong Joon Min ◽  
Joo Hyun Park ◽  
Jung Ho Park ◽  
Jong Min Park
Keyword(s):  

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev

SummaryIt was found that the effect of heparin on the amidase activity of urokinase (E C 3.4.21.31), plasmin (E C 3.4.21.7) and trypsin (E C 3.4.21.4) depended on the substrate used. No effect of heparin on the amidase activity of urokinase and trypsin was observed when Pyro Glu-Gly-Arg-p-nitroanilide (S-2444) and α-N-acetyl-L-lysine-p-nitroanilide (ALNA) were used as substrates. Heparin acted as a uncompetitive inhibitor of trypsin (Ki = 1.2×10-6 M), plasmin (Ki = 4.9×10-6 M) and urokinase (Ki = l.0×10-7 M) when Bz-Phe-Val-Arg-p-nitroanilide (S-2160), H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and plasminogen, respectively, were used as substrates. These results, as well as the data obtained by studying the effect of the simultaneous presence of heparin and competitive inhibitors suggest that although heparin is not bound at the active center of these enzymes, it may influence the effectivity of catalysis.


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