Purification of the putative hormone-sensitive cyclic AMP phosphodiesterase from rat adipose tissue using a derivative of cilostamide as a novel affinity ligand.
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چکیده
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Purification of the putative hormone-sensitive cyclic AMP phosphodiesterase from rat adipose tissue using a derivative of cilostamide as a novel affinity ligand.
A "low Km" cAMP phosphodiesterase with properties of a peripheral membrane protein accounts for approximately 90% of total cAMP phosphodiesterase activity in particulate (100,000 X g) fractions from rat fat cells. Incubation of fat cells with insulin for 10 min increased particulate (but not soluble) cAMP phosphodiesterase activity, with a maximum increase (approximately 100%) at 1 nM insulin. ...
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15 صفحه اولInsulin-dependent and insulin-independent low Km cyclic AMP phosphodiesterase from rat adipose tissue.
Chromatographic analysis of a soluble extract of rat adipose tissue on DEAE-Sephacel resolves four distinct peaks of 3':5'-nucleotide phosphodiesterase (EC 3.1.4.17) activity. Kinetic investigation indicates that two of these fractions have a high affinity for cyclic AMP and show negative cooperative kinetic behavior at high substrate concentration. They differ in the degree of inhibition by cy...
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15 صفحه اولPurification to homogeneity and general properties of a novel phosphodiesterase hydrolyzing cyclic CMP and cyclic AMP.
A cytidine 3’5’-monophosphate (cyclic CMP) phosphodiesterase was purified more than 10,000-fold to apparent homogeneity from the pig liver extract by the steps of pH and ammonium sulfate fractionations, and DEAE-cellulose, Sephadex G-100, and 8-HzN(CH&NHcyclic AMP Sepharose 4B affinity chromatographies. The preparation appeared as a single protein band in sodium dodecyl sulfate-polyacrylamide g...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1987
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)45645-1