Partial purification and characterization of cyclic nucleotide phosphodiesterases from human bronchial tissue.
DEAE-Sephadex chromatography reveals the presence in extracts of human bronchial tissue of at least three separate cyclic nucleotide phosphodiesterases: a cyclic GMP-specific high affinity enzyme, a non-specific low affinity enzyme, and a high affinity cyclic AMP-specific enzyme. The activity of each fraction was partially characterized with respect to kinetic parameters, thermal stability, and the influence of a number of inhibitors. Each activity was found to resemble the activity of the previously characterized corresponding enzyme from whole lung tissue extracts. A high affinity non-specific phospho-diesterase previously isolated from lung tissue is missing in extracts of bronchial tissue.
D015105:3',5'-Cyclic-AMP Phosphodiesterases / Q000302:isolation & purification* / Q000378:metabolism; D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000302:isolation & purification* / Q000378:metabolism; D001980:Bronchi / Q000201:enzymology*; D002277:Carcinoma / Q000378:metabolism; D002852:Chromatography, Ion Exchange; D004791:Enzyme Inhibitors / Q000494:pharmacology; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D008168:Lung / Q000201:enzymology; D008175:Lung Neoplasms / Q000378:metabolism
D004791:Enzyme Inhibitors; D015105:3',5'-Cyclic-AMP Phosphodiesterases; D015106:3',5'-Cyclic-GMP Phosphodiesterases