Regulation of cyclic adenosine 3':5'-monophosphate phosphodiesterases. Interrelationship of the various forms in rat skeletal myoblasts and adult muscle

The authors report in this paper the purification of PDE I and PDE IV from rat skeletal muscle and myoblasts, and a comparison of their kinetic properties and subunit structure. The evidence presented favors the view that myoblasts have only one primary form of phosphodiesterase (PDE II) which can b...

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Bibliographic Details
Published in:The Journal of biological chemistry 1982-04, Vol.257 (8), p.4618-4626
Main Authors: Narindrasorasak, S, Tan, L U, Seth, P K, Sanwal, B D
Format: Article
Language:English
Subjects:
3',5'-Cyclic-AMP Phosphodiesterases - isolation & purification
3',5'-Cyclic-AMP Phosphodiesterases - metabolism
3':5'-cyclic-nucleotide phosphodiesterase
Amino Acids - analysis
Animals
Cell Differentiation
Cell Line
Chymotrypsin - metabolism
Enzyme Activation
Kinetics
Molecular Weight
Muscles - enzymology
purification
Rats
skeletal muscle
Trypsin
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Summary:The authors report in this paper the purification of PDE I and PDE IV from rat skeletal muscle and myoblasts, and a comparison of their kinetic properties and subunit structure. The evidence presented favors the view that myoblasts have only one primary form of phosphodiesterase (PDE II) which can be converted in vitro on one hand to PDE I by aggregation and on the other to PDE IV by proteolysis.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)34769-0