Cloning and expression of cDNA for a human low-K sub(m), rolipram-sensitive cyclic AMP phosphodiesterase

We have isolated cDNA clones representing cyclic AMP (cAMP)-specific phosphodiesterase (PDEases) from a human monocyte cDNA library. One cDNA clone (hPDE-1) defines a large open reading frame of ca. 2.1 kilobases, predicting a 686-amino-acid, ca. 77-kilodalton protein which contains significant homo...

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Published inMolecular and cellular biology Vol. 10; no. 6; pp. 2678 - 2686
Main Authors Livi, G P, Kmetz, P, McHale, M M, Cieslinski, L B, Sathe, G M, Taylor, D P, Davis, R L, Torphy, T J, Balcarek, J M
Format Journal Article
LanguageEnglish
Published 01.01.1990
Subjects
man
monocytes
phosphodiesterase I
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Summary:We have isolated cDNA clones representing cyclic AMP (cAMP)-specific phosphodiesterase (PDEases) from a human monocyte cDNA library. One cDNA clone (hPDE-1) defines a large open reading frame of ca. 2.1 kilobases, predicting a 686-amino-acid, ca. 77-kilodalton protein which contains significant homology to both rat brain and Drosophila cAMP PDEases, especially within an internal conserved domain of ca 270 residues. Amino acid sequence divergence exists at the NH sub(2) terminus and also within a 40- to 100-residue domain near the COOH-terminal end.
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ISSN:0270-7306