Cyclic nucleotide phosphodiesterase activities in rat erythrocytes

Erythrocyte soluble phosphodiesterase activities show at least two interconvertible states: 'aggregated' and 'non-aggregated'. In the former state the existence of a high affinity component for cyclic AMP is favoured and the system is more active with cyclic AMP than with cyclic...

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Guardado en:
Detalles Bibliográficos
Publicado: 1982
Materias:
cyclic amp
cyclic gmp
cyclic nucleotide phosphodiesterase
animal experiment
blood and hemopoietic system
erythrocyte
rat
3',5'-Cyclic-GMP Phosphodiesterase
3',5'-Cyclic-Nucleotide Phosphodiesterase
Animal
Chromatography, Gel
Erythrocytes
Isoelectric Focusing
Kinetics
Magnesium
Magnesium Chloride
Male
Rats
Rats, Inbred Strains
Support, Non-U.S. Gov't
Acceso en línea:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03008177_v43_n3_p161_TellezInon
http://hdl.handle.net/20.500.12110/paper_03008177_v43_n3_p161_TellezInon
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario:Erythrocyte soluble phosphodiesterase activities show at least two interconvertible states: 'aggregated' and 'non-aggregated'. In the former state the existence of a high affinity component for cyclic AMP is favoured and the system is more active with cyclic AMP than with cyclic GMP as substrate. When the system is in the 'non-aggregated state', no activity with cyclic GMP is detected. Conversion to the 'non-aggregated state' is enhanced by dilution or by addition of magnesium ions. Upon isoelectric focusing of erythrocyte soluble extracts, phosphodiesterase activities can be resolved in two peaks: one specific for cyclic AMP located at pH 4.66 and the other specific for cyclic GMP focused at pH 4.95. Evidence would indicate that aggregation affects the enzyme specific for cyclic AMP. © 1982 Martinus Nijhoff/Dr W. Junk Publishers.

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