Oxidation of Diisopropylamine and Bis(2-Hydroxy Propylamine) by Potassium Peroxydisulfate—A Kinetic Study

1977 ◽  
Vol 258O (1) ◽  
Author(s):  
J. Sreekantha Babu ◽  
Km. Veena Joshi ◽  
A. K. Bhattacharya
Keyword(s):  
Kinetic Study ◽  
Potassium Peroxydisulfate

Kinetic study on degradation of tylosin in aqueous media using potassium peroxydisulfate in the presence of immobilized nanosilver

2014 ◽  
Vol 57 (8) ◽  
pp. 3552-3558
Author(s):  
S. Kamali Moghaddam ◽  
M.H. Rasoulifard ◽  
M. Vahedpour ◽  
M.R. Eskandarian
Keyword(s):  
Kinetic Study ◽  
Aqueous Media ◽  
Potassium Peroxydisulfate

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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