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Molecular Pharmacology

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Research ArticleArticle

Adenosine Triphosphate-Guanosine 5'-Phosphate Phosphotransferase

II. Inhibition by 6-Thioguanosine 5'-Phosphate of the Enzyme Isolated from Hog Brain and Sarcoma 180 Ascites Cells

R. P. MIECH, RICHARD YORK and R. E. PARKS JR.
Molecular Pharmacology January 1969, 5 (1) 30-37;
R. P. MIECH
Division of Biological and Medical Sciences, Brown University, Providence, Rhode Island 02912
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RICHARD YORK
Division of Biological and Medical Sciences, Brown University, Providence, Rhode Island 02912
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R. E. PARKS JR.
Division of Biological and Medical Sciences, Brown University, Providence, Rhode Island 02912
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Abstract

Sarcoma 180 cells contain a highly specific guanylate kinase (ATP-GMP phosphotransferase, EC 2.7.4.8) that converts GMP to GDP. This tumor enzyme closely resembles in its kinetic parameters and molecular size the guanylate kinase of hog brain. With both enzymes the analogue nucleotide 6-thioguanosine 5'-phosphate behaves as a potent inhibitor, competitive with GMP, with an inhibition constant (Ki) of about 6 x 10-5 M. When examined with large amounts of hog brain enzyme, 6-thioguanosine 5'-phosphate behaves as an alternative substrate with a very low maximum velocity that is less than 0.04% of the reaction rate attainable with GMP as the substrate. The possible role of these findings in the cytolytic action of 6-thioguanine is discussed.

  • Copyright ©, 1969, by Academic Press Inc.

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Molecular Pharmacology
Vol. 5, Issue 1
1 Jan 1969
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Research ArticleArticle

Adenosine Triphosphate-Guanosine 5'-Phosphate Phosphotransferase

R. P. MIECH, RICHARD YORK and R. E. PARKS
Molecular Pharmacology January 1, 1969, 5 (1) 30-37;

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Research ArticleArticle

Adenosine Triphosphate-Guanosine 5'-Phosphate Phosphotransferase

R. P. MIECH, RICHARD YORK and R. E. PARKS
Molecular Pharmacology January 1, 1969, 5 (1) 30-37;
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