Further investigations of the transient kinetics of alcohol oxidation catalysed by horse liver alcohol dehydrogenase

1977 ◽  
Vol 114 (2) ◽  
pp. 267-279 ◽  
Author(s):  
Antonio Baici ◽  
Pier Luigi Luisi
Keyword(s):  
Alcohol Dehydrogenase ◽  
Alcohol Oxidation ◽  
Transient Kinetics ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Kinetics Of

Utilization of a recyclization reaction for the analysis of the mechanism of enzymic alcohol oxidation

1982 ◽  
Vol 47 (9) ◽  
pp. 2561-2567 ◽  
Author(s):  
Jan Kovář ◽  
Igor Kučera
Keyword(s):  
Alcohol Dehydrogenase ◽  
Kinetic Parameters ◽  
Alcohol Oxidation ◽  
Point Of View ◽  
Experimental Point ◽  
Recyclization Reaction ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Kinetics Of

The kinetics of recyclization reactions catalyzed by horse liver alcohol dehydrogenase in the presence of a coenzyme, p-nitrosodimethylaniline, and various alcohols was studied from theoretical and experimental point of view. It was found that p-nitrosodimethylaniline is an oxidized substrate of the alcohol dehydrogenase suitable for testing basic kinetic parameters of various alcohols, especially for checking the kinetic importance of ternary enzyme-NAD-alcohol complexes.

Analysis of one enzyme recyclization system with low enzyme concentration

1982 ◽  
Vol 47 (12) ◽  
pp. 3339-3347
Author(s):  
Jan Kovář ◽  
Igor Kučera
Keyword(s):  
Alcohol Dehydrogenase ◽  
Enzyme Concentration ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Horse Liver ◽  
Kinetics Of ◽  
Analytical Practice

One enzyme recyclization reactions in the presence of two substrates and a small amount of a coenzyme are characterized by a long prestationary phase, in the course of which the distribution of coenzyme forms varies. The kinetics of the coenzyme prestationary phase was analyzed theoretically and some equations characterizing mainly the start and the end of this phase were derived. To verify experimentally the derived equations two recyclization systems with horse liver alcohol dehydrogenase, NAD or NADH, and corresponding substrate pairs (p-nitrosodimethylaniline and 1-butanol, or furyl alcohol and acetaldehyde) were investigated. Consequences for the analytical practice and utilization of these reactions for the determination of small coenzyme and enzyme concentrations are discussed.

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