Kinetic study of methoxide-promoted elimination reactions of some 1,1,1-trichloro-2,2-bis(phenyl-substituted)ethanes

2001 ◽  
Vol 15 (2) ◽  
pp. 108-114 ◽  
Author(s):  
Gianfranco Fontana ◽  
Vincenzo Frenna ◽  
Liliana Lamartina ◽  
Maria Concetta Natoli ◽  
Renato Noto
Keyword(s):  
Kinetic Study ◽  
Elimination Reactions

Kinetic study of base-promoted elimination reactions of some 1,1,1-trihalo-2,2-bis(dimethoxyphenyl)ethanes in alcoholic solutions

1998 ◽  
Vol 11 (1) ◽  
pp. 54-58 ◽  
Author(s):  
Gianfranco Fontana ◽  
Vincenzo Frenna ◽  
Michelangelo Gruttadauria ◽  
Maria Concetta Natoli ◽  
Renato Noto
Keyword(s):  
Kinetic Study ◽  
Elimination Reactions

Carbonyl-forming elimination reactions. A kinetic study of the decomposition of β-nitroalcohols in water

1980 ◽  
Vol 21 (49) ◽  
pp. 4735-4738 ◽  
Author(s):  
G. Guanti ◽  
G. Petrillo ◽  
S. Thea ◽  
G. Cevasco ◽  
C.J.M. Stirling
Keyword(s):  
Kinetic Study ◽  
Elimination Reactions

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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