Kinetic study of the oxidation of aliphatic aldehydes bybis(2,2′-bipyridyl) copper(II) permanganate

1992 ◽  
Vol 104 (5) ◽  
pp. 583-589
Author(s):  
Seema Kothari ◽  
Vinita Sharma ◽  
Pradeep K. Sharma ◽  
Kalyan K. Banerji
Keyword(s):  
Kinetic Study ◽  
Aliphatic Aldehydes

Kinetic study of OH and NO3 radical reactions with 14 aliphatic aldehydes

2001 ◽  
Vol 3 (15) ◽  
pp. 3057-3063 ◽  
Author(s):  
Barbara D'Anna ◽  
Øyvind Andresen ◽  
Ziv Gefen ◽  
Claus J. Nielsen
Keyword(s):  
Kinetic Study ◽  
Radical Reactions ◽  
Aliphatic Aldehydes ◽  
No3 Radical

A PLP–LIF kinetic study of the atmospheric reactivity of a series of C4–C7 saturated and unsaturated aliphatic aldehydes with OH

2002 ◽  
Vol 36 (20) ◽  
pp. 3231-3239 ◽  
Author(s):  
José Albaladejo ◽  
Bernabé Ballesteros ◽  
Elena Jiménez ◽  
Pilar Martı́n ◽  
Ernesto Martı́nez
Keyword(s):  
Kinetic Study ◽  
Aliphatic Aldehydes ◽  
Atmospheric Reactivity

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.

A kinetic study of the metathesis of propene on a rhenium-aluminium catalyst

1981 ◽  
Vol 31 (1) ◽  
pp. 388-394 ◽  
Author(s):  
Mahmoud El-Sawi ◽  
Antonio Iannibello ◽  
Fernando Morelli ◽  
Ganfranco Gatalano ◽  
Francesco Intrieri ◽  
...  
Keyword(s):  
Kinetic Study
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