Manganese ion dependent adenylate cyclase activity in rat testes: purification and properties.

Testicular, soluble adenylate cyclase has been purified by anion-exchange chromatography, gel filtration, and isoelectric focusing. Upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peak fractions from the latter purification step showed only one polypeptide band with an apparent molecular weight of about 69 000. The following hydrodynamic and molecular parameters have been established for this enzyme: sedimentation constant, 4.3; Stokes radius, 3.95 nm; partial specific volume, 0.74 mL.g(-1); molecular weight, 74 000; fractional ratio, 1.4.