Oxidation of l -Hydroxyproline by Aqueous Alkaline Permanganate--A Kinetic Study

2002 ◽  
Vol 4 (1-2) ◽  
pp. 67-76 ◽  
Author(s):  
Sairabanu A. Farokhi ◽  
A.K. Kini ◽  
S.T. Nandibewoor
1981 ◽  
Vol 59 (18) ◽  
pp. 2776-2779 ◽  
Author(s):  
Donald G. Lee ◽  
Carlos F. Sebastián

A kinetic study has been made of the oxidation of phenol and seven chlorophenols by alkaline permanganate. The initial reaction, which results in the formation of manganate(VI) ion, is first order with respect to permanganate ion, independent of the concentration of hydroxide ion, and of variable order with respect to phenol. At low phenol concentrations the order is unity, but at high concentrations it becomes zero. These observations can be accounted for quantitatively by the following mechanism:[Formula: see text]


2002 ◽  
Vol 2002 (11) ◽  
pp. 533-534 ◽  
Author(s):  
P.D. Pol ◽  
R.T. Mahesh ◽  
S.T. Nandibewoor

The reaction proceeds in two different stages. A mechanism is proposed and the constants involved in the mechanism are evaluated. The activation parameters for the slow step were calculated and are discussed.


2019 ◽  
Vol 9 (1) ◽  
pp. 159-164
Author(s):  
Narayan V. Lawale ◽  
Bhagwan Singh Dobhal ◽  
Sandip Singh Gaur ◽  
Rajendra Pardeshi

Permanganatic oxidation of Neomycine sulphate salt has been studied at different temperatures using spectrophotometer under alkaline conditions. The effect of variation of substrate Neomycine sulphate salt (NS), oxidant (KMnO4) and NaOH was studied under pseudo first order reaction conditions. The effect of different salts and solvents on oxidation of NS was also studied. The reaction was found to be first order with respect to oxidant, substrate and NaOH.. Keywords: Neomycine sulphate salt (NS), KMnO4 , permanganatic  oxidation, alkaline permanganate


1999 ◽  
Vol 1 (3) ◽  
Author(s):  
Md. Saleem R. Kembhavi ◽  
Rafeek G. Panari ◽  
Sharanappa T. Nandibewoor

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):  

1983 ◽  
Vol 49 (03) ◽  
pp. 199-203 ◽  
Author(s):  
V M Yomtova ◽  
N A Stambolieva ◽  
B M Blagoev

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.


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

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