title: Epiphyseal cartilage cyclic nucleotide phosphodiesterase: partial purification and kinetic characteristics of multiple enzymes.
abstract: Partial purification of chicken epiphyseal PDE activity by centrifugation and column chromatography has defined two distinct peaks of PDE activity. The faster eluting peak (I) has a higher apparent Km for cyclic AMP than the slower eluting major peak (IIs and II). Peak I has greater activity towards cyclic AMP as a substrate than towards cyclic GMP but does use both substrates. Peak I is not inhibited by T-3 or indomethacin at physiological concentrations. Substrates studies demonstrate the presence of at least two overlapping PDE species in the major peak(IIs and II). There is suggestive evidence that indomethacin is a more potent inhibitor of peak IIs which can use either cyclic AMP or cyclic GMP as substrates, whereas T-3 is a more potent inhibitor of fractions eluting where the enzyme only has activity with cyclic AMP.
mesh_terms: D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002356:Cartilage / Q000201:enzymology*; D002645:Chickens; D000242:Cyclic AMP / Q000378:metabolism; D006152:Cyclic GMP / Q000378:metabolism; D004838:Epiphyses / Q000201:enzymology*; D007213:Indomethacin / Q000494:pharmacology; D007700:Kinetics; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D014284:Triiodothyronine / Q000494:pharmacology
chemical_list: D014284:Triiodothyronine; D000242:Cyclic AMP; D010727:Phosphoric Diester Hydrolases; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D006152:Cyclic GMP; D007213:Indomethacin