Kinetic study of the oxovanadium(IV)–salen-catalyzed H2O2 oxidation of phenols

2015 ◽  
Vol 40 (4) ◽  
pp. 355-362 ◽  
Author(s):  
Alagarsamy Mathavan ◽  
Arumugam Ramdass ◽  
Seenivasan Rajagopal
Keyword(s):  
Kinetic Study ◽  
H2o2 Oxidation ◽  
Oxidation Of Phenols

scholarly journals Stopped-flow kinetic study of the H2O2 oxidation of substrates catalyzed by microperoxidase-8

2001 ◽  
Vol 6 (8) ◽  
pp. 770-777 ◽  
Author(s):  
Hui-Chun Yeh ◽  
Jinn-Shyan Wang ◽  
Oliver Y. Su ◽  
Wann-Yin Lin
Keyword(s):  
Kinetic Study ◽  
Stopped Flow ◽  
H2o2 Oxidation ◽  
Microperoxidase 8

A kinetic study of the oxidation of phenols and chlorophenols by metaperiodate

1983 ◽  
Vol 153 ◽  
pp. 285-290 ◽  
Author(s):  
N.G. Buckman ◽  
R.J. Magee ◽  
J.O. Hill
Keyword(s):  
Kinetic Study ◽  
Oxidation Of Phenols

UV–H2O2 oxidation of monoazo dyes in aqueous media: a kinetic study

1999 ◽  
Vol 40 (1) ◽  
pp. 27-35 ◽  
Author(s):  
C. Galindo ◽  
A. Kalt
Keyword(s):  
Kinetic Study ◽  
Aqueous Media ◽  
H2o2 Oxidation ◽  
Monoazo Dyes

A kinetic study of osmium tetroxide catalysed oxidation of methyl digol and ethyl digol by hexacyanoferrate (III) in aqueous alkaline medium

1976 ◽  
Vol 73 ◽  
pp. 283-286 ◽  
Author(s):  
H. S. Singh ◽  
A. K. Sisodia ◽  
S. M. Singh ◽  
R. K. Singh ◽  
R. N. Singh
Keyword(s):  
Kinetic Study ◽  
Alkaline Medium ◽  
Osmium Tetroxide ◽  
Aqueous Alkaline Medium ◽  
Catalysed Oxidation

A kinetic study of controlling nitrogen in process for boron steel by using30N2isotope gas

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):  
Kinetic Study ◽  
Boron Steel

Kinetic Study of the Effect of Heparin on the Amidase Activity of Trypsin, Plasmin and Urokinase

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev
Keyword(s):  
Kinetic Study ◽  
Active Center ◽  
Simultaneous Presence ◽  
Amidase Activity ◽  
Competitive Inhibitors ◽  
Uncompetitive Inhibitor

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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