The effect of magic number phosphine stabilised mono- and bimetallic Au, Cu and Au-Cu nanoparticles as catalysts in the reduction of 4-nitrophenol–A kinetic study

Kinetic study of the reaction of benzoyl peroxide with phenolic compounds. A technique for the evaluation of phenolic O-H bond dissociation energies

Journal de Chimie Physique ◽

10.1051/jcp/1989862057 ◽

1989 ◽

Vol 86 ◽

pp. 2057-2066 ◽

Cited By ~ 2

Author(s):

Claire Rousseau-Richard ◽

Claude Richard ◽

René Martin

Keyword(s):

Phenolic Compounds ◽

Kinetic Study ◽

Benzoyl Peroxide ◽

Bond Dissociation Energies ◽

Bond Dissociation ◽

Dissociation Energies

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

Journal de Chimie Physique ◽

10.1051/jcp/1976730283 ◽

1976 ◽

Vol 73 ◽

pp. 283-286 ◽

Cited By ~ 2

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

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

Revue de Métallurgie ◽

10.1051/metal:2009004 ◽

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

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

Thrombosis and Haemostasis ◽

10.1055/s-0038-1657362 ◽

1983 ◽

Vol 49 (03) ◽

pp. 199-203 ◽

Cited By ~ 10

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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