Solubilization and other studies on adenylate cyclase of baker's yeast.
1. Adenylate cyclase of Saccharomyces cerevisiae was sedimented from mechanically disintegrated preparations of yeast over an unusually wide range of centrifugal forces. 2. The enzyme was readily solubilized by Ficoll and by Lubrol PX. Lubrol caused a 2-fold activation. 3. Both particle-bound and Lubrol-solubilized enzyme had an apparent Km for ATP of 1.6 mM in the presence of 0.4 mM-cyclic AMP and 5 mM-MnCl2 at pH 6.2 and 30 degrees C. 4. The Lubrol-solubilized enzyme behaved on gel filtration as a monodisperse protein with an apparent mol.wt. of about 450000.
D000262:Adenylyl Cyclases / Q000302:isolation & purification*; D002458:Cell Fractionation; D002467:Cell Nucleus / Q000201:enzymology; D003902:Detergents; D005362:Ficoll; D007700:Kinetics; D008274:Magnesium; D008345:Manganese; D011092:Polyethylene Glycols; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D012995:Solubility; D013104:Spheroplasts / Q000302:isolation & purification
D003902:Detergents; D005362:Ficoll; D011092:Polyethylene Glycols; D008345:Manganese; D000262:Adenylyl Cyclases; D008274:Magnesium