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 in | Molecular and cellular biology Vol. 10; no. 6; pp. 2678 - 2686 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
01.01.1990
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Subjects | |
Online Access | Get full text |
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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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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-2 |
ISSN: | 0270-7306 |