Identification of ATP citrate lyase as a phosphoprotein.

摘要: ATP citrate lyase has been purified from rat liver by a new procedure which results in high yields of an intact and stable enzyme. The pure (specific activity approximately equal to 10 at 25 degrees C) exhibits single protein band upon sodium dodecyl sulfate (SDS)-gel electrophoresis (Mr = 110,000). This minimizes protease degradation that usually occurs when the enzyme is isolated previously described isolation methods. In addition, shown be phosphoprotein. 32P-labeled following intraperitoneal injection inorganic [32P]phosphate into animals. It demonstrated this phosphate (structural phosphate) behaves as serine not same enzyme-bound (catalytic derived during reaction. There are 2 structural residues for each tetramer molecule. Removal accomplished using partially phosphatase liver. dephospholyase Vmax native phosphoenzyme. Evidence indicates resides protease-sensitive region