The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Determination of the kinetic parameters of adenosine deaminase by electrophoretically mediated microanalysis.

The possibility of determining the Michaelis constant of the irreversible deamination of adenosine to inosine by adenosine deaminase, using capillary electrophoresis, was investigated. This paper describes the use of electrophoretically mediated microanalysis (EMMA) as the technique for carrying out the assay. Initial reaction velocities of the enzymatic reaction were estimated from the peak area of inosine, and the Michaelis constant was calculated according to the Lineweaver-Burk equation. The result (Km = 5.3 x 10(-5) M +/- 8 x 10(-6) M) was consistent with previously reported values. Using the present method, a total amount of as few as 1.2 fmole of enzyme and 9.2 ng of substrate were injected in the capillary for the construction of a Michaelis Menten curve (seven concentrations of substrate, each concentration analyzed in triplicate), which is far smaller than the quantities required in conventional methods.[1]

References

  1. Determination of the kinetic parameters of adenosine deaminase by electrophoretically mediated microanalysis. Saevels, J., Van Schepdael, A., Hoogmartens, J. Electrophoresis (1996) [Pubmed]
 
WikiGenes - Universities