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

Changing activities of galactose-metabolizing enzymes during perfusion of suckling-rat liver.

The specific activities of the galactose-metabolizing enzymes, galactokinase (EC, galactose-1-phosphate uridyltransferase (EC, and UDPgalactose 4-epimerase (EC, in suckling-rat livers perfused for 90 min with 1 and 4 mM galactose fluctuate significantly with a different pattern of change for each enzyme. Perfusion for 30 min with galactose resulted in a significant increase of transferase specific activity followed by a precipitous decline to about one-fifth of the activity in unperfused liver at 90 min. The increase in transferase activity was also observed when D-glucose was perfused but not when L-glucose, D-fructose, D-xylose, or D-ribose was added to the perfusate. No such changes in transferase activity were observed when adult-rat liver was perfused with galactose. Epimerase activity in the suckling-rat liver was relatively low, and the changes in its activity correlated best with the uptake rate of galactose. The perfused suckling-rat liver may provide a model system for examination of factors that modulate the specific activity of galactose-metabolizing enzymes and effect the metabolism of galactose.[1]


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