Purification and some properties of ATP-citrate lyase from rat brain.
ATP-citrate lyase has been purified from rat brain by a new procedure which yields an enzyme of specific activity of 21 U/mg protein (37 degrees C) (2050-fold purification). Purity (by sodium dodecyl sulfate-gel electrophoresis) of the preparation was comparable to that of rat liver ATP-citrate lyase of similar specific activity. Both brain and liver ATP-citrate lyase have the same electrophoretic mobility, as well as the same immunoreactivity against specific rabbit anti-rat liver ATP-citrate lyase antibody. These data indicate that rat brain ATP-citrate lyase is similar or identical to that present in rat liver. Intraperitoneally injected 32Pi was incorporated into the structural phosphate of ATP-citrate lyase in rat liver but not into the rat brain enzyme.
D001275:ATP Citrate (pro-S)-Lyase / Q000276:immunology / Q000302:isolation & purification*; D000818:Animals; D001921:Brain / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008099:Liver / Q000201:enzymology; D008297:Male; D011817:Rabbits; D051381:Rats; D011919:Rats, Inbred Strains; D012967:Sodium Dodecyl Sulfate
D012967:Sodium Dodecyl Sulfate; D001275:ATP Citrate (pro-S)-Lyase