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[Purification and properties of cyclic nucleotide phosphodiesterase from uterine tissue]
Biokhimiia (Moscow, Russia)
|August 1, 1988
Abstract:
Cyclic nucleotide phosphodiesterase from calf myometrium has been purified to a homogeneous state for the first time, as can be evidenced from polyacrylamide gel electrophoresis data. The purification procedure included ion-exchange chromatography on DEAE-cellulose, high pressure liquid chromatography on TSK 545 DEAE and gel filtration through Toyopearl HW-55. The molecular mass of the enzyme as determined by gel filtration and polyacrylamide gel electrophoresis is 110 kD. The purified enzyme hydrolyzes cAMP and cGMP with Km = 30 microM and 18 microM, respectively.