cAMP analogs and selective inhibitors used to study low Km Mucor rouxii cAMP phosphodiesterase
1. 1. The sensitivity of partially purified low Km, phosphodiesterase (PDE) from Mucor rouxii to pharmacological agents and cAMP analogs was studied. The IC50 obtained were compared with those reported for PDEs from higher eukaryotes. 2. 2. The best inhibitors of the hydrolysis of 1 gmM cAMP were SQ...
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Autores principales: | , |
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Formato: | JOUR |
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Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_0020711X_v22_n9_p1047_Tomes |
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Sumario: | 1. 1. The sensitivity of partially purified low Km, phosphodiesterase (PDE) from Mucor rouxii to pharmacological agents and cAMP analogs was studied. The IC50 obtained were compared with those reported for PDEs from higher eukaryotes. 2. 2. The best inhibitors of the hydrolysis of 1 gmM cAMP were SQ 65.442 (IC50, c 10 μM), dipyridamol and CI 930. cGMP was not an inhibitor (IC50 > 1000 μm). 3. 3. The cAMP analogs were tested as inhibitors of the hydrolysis of 0. l μM cAMP. 8-Aminohexylamino cAMP was the best inhibitor with an IC50 of c 1 μM. 4. 4. A sedimentation profile of Mucor PDE was assayed in the presence of several pharmacological inhibitors and eAMP analogs. No isoforms with different sensitivity towards the inhibitors were detected. Forms with slightly different behaviour towards some cAMP analogs were observed. © 1990. |
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