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HERO ID
3227796
Reference Type
Journal Article
Title
Solubilization and characterization of hormone- responsive phosphodiesterase activity of rat fat cells
Author(s)
Lovell-Smith, CJ; Manganiello, VC; Vaughan, M
Year
1977
Is Peer Reviewed?
1
Journal
Biochimica et Biophysica Acta
ISSN:
0006-3002
EISSN:
1878-2434
Volume
497
Issue
2
Page Numbers
447-458
Language
English
PMID
192314
Abstract
Fat cells particulate phosphodiesterase activity can be solubilized in high yield (80--100%) in a buffer system (30 mM Tris - HCl, pH 8.0) containing non-ionic detergents (0.1% Brij 30, 1.0% Triton X-100), salt (3.0 mM MgSO4, 5.0 mM NaBr) and dithiothreitol (5.0 mM). Polyacrylamide gel electrophoresis of the solubilized enzyme activity indicated the presence of two bands of activities of different electrophoretic mobilities, both of which hydrolyzed cyclic AMP and cyclic GMP. The solubilized activity eluted from DEAE Bio-Gel columns as a somewhat broad profile with at least two peaks of activity. Activity against both cyclic AMP and cyclic GMP eluted in similar but not identical patterns. The solubilized enzyme and DEAE column eluates wxhibited low (less than 1 micronM) Michaelis constants for cyclic AMP and cyclic GMP. In addition, the increases in phosphodiesterase activity induced by incubation of intact fat cells with insulin or adrenocorticotropic hormone are maintained in the solubilized state.
Tags
NAAQS
•
ISA-PM (2019)
Considered
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