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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Inhibitory effect of ethanol administration on beta-alanine-2-oxoglutarate aminotransferase (GABA aminotransferase) in disulfiram-pretreated rats.

Ethanol in the presence of disulfiram (N,N,N',N'-tetraethylthiuram disulfide, an inhibitor of aldehyde dehydrogenase) inhibited liver beta-alanine-oxoglutarate aminotransferase (beta-AlaAT I) activity yet activated tyrosine aminotransferase ( TAT) in weanling rats in vivo. The effect on beta-AlaAT I was followed by the inhibitory expression of beta-AlaAT I mRNA. The beta-AlaAT I activity was reduced with a pseudo-first-order profile with time, and the half-life was calculated to be 12.3 +/- 0.83 h with the rate constant (Kd) of 0.056 +/- 0.004 h-1. The synthesis of beta-AlaAT I in rat liver was estimated to be 1.56 x 10(-10) mol/g of wet tissue per hour at a steady state. A combination of ethanol and disulfiram also reduced beta-alanine-pyruvate aminotransferase (beta-AlaAT II) activity to 60% of the control after 24 h.[1]

References

  1. Inhibitory effect of ethanol administration on beta-alanine-2-oxoglutarate aminotransferase (GABA aminotransferase) in disulfiram-pretreated rats. Kontani, Y., Kawasaki, S., Kaneko, M., Matsuda, K., Sakata, S.F., Tamaki, N. J. Nutr. Sci. Vitaminol. (1998) [Pubmed]
 
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