Kinetic study of the oxidation of thioacids by pyridinium fluorochromate

1991 ◽  
Vol 16 (6) ◽  
pp. 641-644 ◽  
Author(s):  
Kakuli Chowdhury ◽  
Sarswati Agarwal ◽  
Kalyan K. Banerji
Keyword(s):  
Kinetic Study ◽  
Pyridinium Fluorochromate

scholarly journals Kinetic Study on Induced Electron Transfer Reaction in Pentaamminecobalt(III) Complexes of α-Hydroxy Acids by Pyridinium Fluorochromate in Micellar Medium

2011 ◽  
Vol 8 (3) ◽  
pp. 1102-1107
Author(s):  
B. Mohammed Nawaz ◽  
K. Subramani ◽  
Mansur Ahmed
Keyword(s):  
Electron Transfer ◽  
Kinetic Study ◽  
Carbonyl Compounds ◽  
Transfer Reaction ◽  
Electron Transfer Reaction ◽  
Micellar Medium ◽  
Hydroxy Acids ◽  
Uv Visible ◽  
Pyridinium Fluorochromate

Pyridinium fluorochromate (PFC) oxidation of pentaamminecobalt(III) complexes of α-hydroxy acids in micellar medium yielding nearly 100% of carbonyl compounds are ultimate products. The decrease in UV-visible absorbance at λ=502 nm for Co(III) complex corresponds to nearly 100% of the initial absorbance. The stoichiometry of unbound ligand and cobalt(III) complex is accounting for about 100% reduction at the cobalt(III) centre. The kinetic and stoichiometric results have been accounted by a suitable mechanism.

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.

Sign in / Sign up

Export Citation Format

Share Document