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The identification and characterization of two cyclic nucleotide phosphodiesterases from bovine adrenal medulla.
Arch Biochem Biophys. 1986 Aug 15; 249(1):95-105.AB

Abstract

Two soluble cyclic nucleotide phosphodiesterase activities, designated Peak I (Mr = 216,000) and Peak II (Mr = 230,000), have been isolated from bovine adrenal medulla by DEAE-cellulose chromatography. Peak I has Ca2+-independent, cGMP-specific phosphodiesterase activity and Peak II has cGMP-stimulated cyclic nucleotide phosphodiesterase activity. Peak I hydrolyzes cGMP with hyperbolic kinetics and demonstrates a Km of 23 microM. Peak II hydrolyzes cGMP with hyperbolic kinetics but hydrolyzes cAMP with slightly sigmoidal kinetics and demonstrates Km values of 54 +/- 0.7 microM cGMP and 38 +/- 6 microM cAMP. Cyclic AMP and cGMP are competitive inhibitors of each other's hydrolysis, suggesting that these nucleotides may be hydrolyzed at the same catalytic site. Micromolar concentrations of cGMP cause a 5-fold stimulation of the hydrolysis of subsaturating concentrations of cAMP by the Peak II phosphodiesterase. Half-maximal activation occurs at 0.5 microM cGMP and the result of activation is a decrease in the apparent Km for cAMP. Stimulation of the hydrolysis of subsaturating concentrations of cGMP by cAMP was also detected; however, cAMP is a less potent activator of the enzyme than cGMP. Cyclic AMP causes a 1.5-fold stimulation of cGMP hydrolysis and half-maximal activation occurs at 2.5 microM cAMP.

Authors

Sabatine JM
No affiliation info available
Coffee CJ
No affiliation info available

MeSH

3',5'-Cyclic-AMP Phosphodiesterases3',5'-Cyclic-GMP PhosphodiesterasesAdrenal MedullaAnimalsCattleCyclic AMPCyclic GMPDose-Response Relationship, DrugEnzyme ActivationKineticsMolecular WeightSolubilitySubstrate Specificity

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

3017224

Citation

Sabatine, J M., and C J. Coffee. "The Identification and Characterization of Two Cyclic Nucleotide Phosphodiesterases From Bovine Adrenal Medulla." Archives of Biochemistry and Biophysics, vol. 249, no. 1, 1986, pp. 95-105.
Sabatine JM, Coffee CJ. The identification and characterization of two cyclic nucleotide phosphodiesterases from bovine adrenal medulla. Arch Biochem Biophys. 1986;249(1):95-105.
Sabatine, J. M., & Coffee, C. J. (1986). The identification and characterization of two cyclic nucleotide phosphodiesterases from bovine adrenal medulla. Archives of Biochemistry and Biophysics, 249(1), 95-105.
Sabatine JM, Coffee CJ. The Identification and Characterization of Two Cyclic Nucleotide Phosphodiesterases From Bovine Adrenal Medulla. Arch Biochem Biophys. 1986 Aug 15;249(1):95-105. PubMed PMID: 3017224.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The identification and characterization of two cyclic nucleotide phosphodiesterases from bovine adrenal medulla. AU - Sabatine,J M, AU - Coffee,C J, PY - 1986/8/15/pubmed PY - 1986/8/15/medline PY - 1986/8/15/entrez SP - 95 EP - 105 JF - Archives of biochemistry and biophysics JO - Arch Biochem Biophys VL - 249 IS - 1 N2 - Two soluble cyclic nucleotide phosphodiesterase activities, designated Peak I (Mr = 216,000) and Peak II (Mr = 230,000), have been isolated from bovine adrenal medulla by DEAE-cellulose chromatography. Peak I has Ca2+-independent, cGMP-specific phosphodiesterase activity and Peak II has cGMP-stimulated cyclic nucleotide phosphodiesterase activity. Peak I hydrolyzes cGMP with hyperbolic kinetics and demonstrates a Km of 23 microM. Peak II hydrolyzes cGMP with hyperbolic kinetics but hydrolyzes cAMP with slightly sigmoidal kinetics and demonstrates Km values of 54 +/- 0.7 microM cGMP and 38 +/- 6 microM cAMP. Cyclic AMP and cGMP are competitive inhibitors of each other's hydrolysis, suggesting that these nucleotides may be hydrolyzed at the same catalytic site. Micromolar concentrations of cGMP cause a 5-fold stimulation of the hydrolysis of subsaturating concentrations of cAMP by the Peak II phosphodiesterase. Half-maximal activation occurs at 0.5 microM cGMP and the result of activation is a decrease in the apparent Km for cAMP. Stimulation of the hydrolysis of subsaturating concentrations of cGMP by cAMP was also detected; however, cAMP is a less potent activator of the enzyme than cGMP. Cyclic AMP causes a 1.5-fold stimulation of cGMP hydrolysis and half-maximal activation occurs at 2.5 microM cAMP. SN - 0003-9861 UR - https://www.unboundmedicine.com/medline/citation/3017224/The_identification_and_characterization_of_two_cyclic_nucleotide_phosphodiesterases_from_bovine_adrenal_medulla_ DB - PRIME DP - Unbound Medicine ER -