Purification and some properties of ATP-citrate lyase from rat brain |
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| Authors: | Andrzej Szutowicz Paul A Srere |
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| Institution: | 1. Department of Biochemistry, University of Texas Health Science Center, 5323 Harry Hines Boulevard, Dallas, Texas 75235 USA;2. Department of Pre-Clinical Science, Veterans Administration Medical Center, 4500 South Lancaster Road, Dallas, Texas 75216 USA |
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| Abstract: | 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 °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. |
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