MolPharm xPharm- The Comprehensive Pharmacology Reference

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by BAER, H.-P.
Right arrow Articles by DUNCAN, E. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by BAER, H.-P.
Right arrow Articles by DUNCAN, E. L.

Molecular Pharmacology, Vol 2, 67-76, Copyright © 1966 by the American Society for Pharmacology and Experimental Therapeutics

Formation and Deamination of Adenosine by Cardiac Muscle Enzymes

HANS-PETER BAER 1, GEORGE I. DRUMMOND 1, and E. LOVERNE DUNCAN 1

1 Department of Pharmacology, School of Medicine, The University of British Columbia, Vancouver, Canada

The enzymic catabolism of adenylic acid has been studied in rat heart. AMP may be degraded by two routes, one involving dephosphorylation to adenosine followed by deamination to inosine, the other involving deamination to inosinic acid followed by dephosphorylation to inosine. The data are consistent with the role of adenosine as a regulator of coronary flow. The 5'-nucleotidase and adenosine deaminase have been isolated and partially purified from rat heart acetone powder. The deaminase has also been partially purified from red blood cells. ATP is a potent competitive inhibitor of 5'-nucleotidase and could function as a regulator for the production of adenosine. The substrate specificity of adenosine deaminase has been examined. Several adenosine analogs function as competitive inhibitors of both the heart and red cell enzyme. The most potent inhibitors tested were N6-methyladenosine and 6-methoxypurine ribonucleoside. The coronary dilator, Persantin, does not inhibit cardiac adenosine deaminase at concentrations as high as 4 x 10-4 M.

Note:
ACKNOWLEDGMENT This work was supported by a grant from the Medical Research Council of Canada.

Submitted on November 10, 1965




This article has been cited by other articles:


Home page
 J. Bacteriol.Home page
J. L. Seffernick, A. Aleem, J. P. Osborne, G. Johnson, M. J. Sadowsky, and L. P. Wackett
Hydroxyatrazine N-Ethylaminohydrolase (AtzB): an Amidohydrolase Superfamily Enzyme Catalyzing Deamination and Dechlorination
J. Bacteriol., October 1, 2007; 189(19): 6989 - 6997.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. P. Wackett
Evolution of Enzymes for the Metabolism of New Chemical Inputs into the Environment
J. Biol. Chem., October 1, 2004; 279(40): 41259 - 41262.
[Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
J. L. Seffernick, N. Shapir, M. Schoeb, G. Johnson, M. J. Sadowsky, and L. P. Wackett
Enzymatic Degradation of Chlorodiamino-s-Triazine
Appl. Envir. Microbiol., September 1, 2002; 68(9): 4672 - 4675.
[Abstract] [Full Text] [PDF]

Home page
 Appl. Environ. Microbiol.Home page
J. L. Seffernick, G. Johnson, M. J. Sadowsky, and L. P. Wackett
Substrate Specificity of Atrazine Chlorohydrolase and Atrazine-Catabolizing Bacteria
Appl. Envir. Microbiol., October 1, 2000; 66(10): 4247 - 4252.
[Abstract] [Full Text]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
All ASPET Journals Molecular Pharmacology Pharmacological Reviews
Molecular Interventions Drug Metabolism and Disposition

Copyright © 1966 by the American Society for Pharmacology and Experimental Therapeutics