title: [Purification and properties of cyclic nucleotide phosphodiesterase from uterine tissue].
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.
authors.forename: N O
authors.initials: NO
authors.lastname: Artem'ev
authors.forename: M N
authors.initials: MN
authors.lastname: Garnovskaia
authors.forename: I L
authors.initials: IL
authors.lastname: Dunler
mesh_terms: D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases / Q000302:isolation & purification*; D000818:Animals; D002417:Cattle; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007700:Kinetics; D008970:Molecular Weight; D051381:Rats; D013379:Substrate Specificity; D014599:Uterus / Q000201:enzymology*
chemical_list: D015087:2',3'-Cyclic-Nucleotide Phosphodiesterases
vernacular_title: Ochistka i svoĭstva fosfodiésterazy tsiklicheskikh nukleotidov tkani matki.