Evidence for different forms of rat liver fructose 1,6-bisphosphatase.
Purified liver fructose 1,6-bisphosphatase exhibits different forms upon isoelectric focusing. The enzyme focused at pH 5.75, 5.60, and 5.44. Treatment of the enzyme preparation with the catalytic subunit of cAMP-dependent protein kinase and ATP altered the isoelectric focusing profile such that the bands at 5.75 and 5.60 were diminished, the band at 5.44 increased, and two new bands appeared at 5.30, and 5.18. Fructose 1,6-bisphosphatase may be present in rat liver in different forms, one of which is phosphorylated as the enzyme is isolated.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002845:Chromatography / Q000379:methods; D003720:Densitometry; D006597:Fructose-Bisphosphatase / Q000145:classification / Q000302:isolation & purification*; D007525:Isoelectric Focusing; D008099:Liver / Q000201:enzymology*; D010766:Phosphorylation; D051381:Rats
D006597:Fructose-Bisphosphatase