Protein phosphatases active on acetyl-CoA carboxylase phosphorylated by casein kinase I, casein kinase II and the cAMP-dependent protein kinase.
The protein phosphatases in rat liver cytosol, active on rat liver acetyl-CoA carboxylase (ACC) phosphorylated by casein kinase I, casein kinase II and the cAMP-dependent protein kinase, have been partially purified by anion-exchange and gel filtration chromatography. The major phosphatase activities against all three substrates copurify through fractionation and appear to be identical to protein phosphatases 2A1 and 2A2. No unique protein phosphatase active on 32P-ACC phosphorylated by the casein kinases was identified.
Witters
L A
LA
Bacon
G W
GW
D000103:Acetyl-CoA Carboxylase / Q000378:metabolism*; D000818:Animals; D047388:Casein Kinases; D003600:Cytosol / Q000201:enzymology; D008025:Ligases / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D010749:Phosphoprotein Phosphatases / Q000302:isolation & purification / Q000378:metabolism*; D010761:Phosphorus Radioisotopes; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains
D010761:Phosphorus Radioisotopes; D011494:Protein Kinases; D047388:Casein Kinases; D010749:Phosphoprotein Phosphatases; D008025:Ligases; D000103:Acetyl-CoA Carboxylase