title: Purification of the catalytic subunit of adenylate cyclase in vertebrates: state of the art in 1987.
abstract: After 30 years of effort, the mammalian adenylate cyclase catalytic subunit has now been purified. It is a glycoprotein of 155 kDa, representing less than 0.01% of synaptosomal membrane protein. As measured in the presence of forskolin, its specific activity is 10-20 mumol of cAMP X mg-1 X min-1. The enzyme obtained is completely devoid of Gs alpha subunits, and is calmodulin-dependent. The purification procedures involve an affinity chromatography step, either with calmodulin, or with forskolin, or both. If gel filtration precedes the affinity chromatography, two different fractions with high specific enzyme activity are obtained. One contains the 155 kDa protein as the sole component. The other contains, as its major component, a 105 kDa protein. The relationship between the 2 proteins remains to be defined.
mesh_terms: D000262:Adenylyl Cyclases / Q000032:analysis*; D000818:Animals; D002384:Catalysis
chemical_list: D000262:Adenylyl Cyclases