A partial characterization of the cyclic nucleotide phosphodiesterases of Drosophila melanogaster

The cyclic nucleotide phosphodiesterases in crude homogenate, soluble material, and particulate preparations of adult Drosophila melanogaster flies, hydrolyze cyclic AMP with nonlinear kinetics. Cyclic GMP is hydrolyzed by the phosphodiesterases in crude homogenate and soluble material with linear k... Ausführliche Beschreibung

1. Person: Davis, R.L.
Weitere Personen: Kiger, J.A.
Quelle: in Archives of Biochemistry and Biophysics Vol. 203, No. 1 (1980), p. 412-421
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Format: Online-Artikel
Sprache: English
Veröffentlicht: 1980
Beschreibung: Online-Ressource
Online Zugang: Online
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Anmerkung: Copyright: Copyright (c) 2003 Elsevier (USA)
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520 |a The cyclic nucleotide phosphodiesterases in crude homogenate, soluble material, and particulate preparations of adult Drosophila melanogaster flies, hydrolyze cyclic AMP with nonlinear kinetics. Cyclic GMP is hydrolyzed by the phosphodiesterases in crude homogenate and soluble material with linear kinetics. Physical separation techniques of gel filtration, velocity sedimentation, and ion-exchange chromatography reveal that Drosophila soluble fraction contains two major forms of cyclic nucleotide phosphodiesterase. Form I hydrolyzes both cyclic AMP and cyclic GMP. Inhibition experiments suggest that the hydrolysis of both cyclic nucleotides by Form I occurs at a single active site. The K"m's for hydrolysis of both substrates are about 4 μm. This form has a molecular weight of about 168,000 as estimated by gel nitration. Form II cyclic nucleotide phosphodiesterase is specific for cyclic AMP as substrate. Gel filtration indicates that this form has a molecular weight of about 68,000. The K"m for cyclic AMP is about 2 μm. 
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700 1 |a Kiger, J.A. 
773 0 8 |i in  |t Archives of Biochemistry and Biophysics  |d Amsterdam : Elsevier  |g Vol. 203, No. 1 (1980), p. 412-421  |q 203:1<412-421  |w (DE-601)NLEJ177020539  |x 0003-9861 
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