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Molecular Pharmacology, Vol 6, 641-648, Copyright © 1970 by the American Society for Pharmacology and Experimental Therapeutics

Purification and Properties of Rat Heart 5'-Nucleotidase

MERILYN J. EDWARDS 1 and M. HELEN MAGUIRE 1

1 Smith Kline and French Institute, Department of Pharmacology, University of Sydney, Sydney, New South Wales 2006, Australia

5'-Nucleotidase (EC 3.1.3.5) has been purified 26-fold from rat heart and obtained substantially free of nonspecific phosphatase activity. The pH optimum for the enzyme was 7.6; at this pH, 7 mM Mg++ and 2 mM Ca++ caused 40% inhibition of 5'-nucleotidase activity, and 0.17-0.69 mM Mg++ was without effect on activity. The nucleoside triphosphates ATP, UTP, CTP, GTP, and ITP inhibited 5'-nucleotidase in a noncompetitive manner with respect to adenosine 5'-monophosphate. The AMP analogues adenosine 5'-phosphorothioate (AMPS) and 2-chloroadenosine 5'-monophosphate (2-chloro-AMP), which are vasodilators, and 2-methylthioadenosine 5'-monophosphate (2-methylthio-AMP), which has no vasodilatory properties, were all substrates of 5'-nucleotidase, with Michaelis constants similar to that of AMP. The maximum velocities of hydrolysis of AMPS, 2-chloro-AMP, and 2-methylthio-AMP were 36%, 79%, and 116%, respectively, of the maximum velocity for AMP. The rates of hydrolysis of these analogues by 5'-nucleotidase are considered in relation to their vasodilatory effects.

Note:
ACKNOWLEDGMENT The authors wish to thank Dr. W. J. O’Sullivan of the Department of Medicine, University of Sydney, for his calculations of MgAMP concentrations.

Submitted on August 13, 1970




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