Clinical Chemistry
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Clinical Chemistry 30: 1555-1557, 1984;
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Clinical Chemistry, Vol 30, 1555-1557, Copyright © 1984 by American Association for Clinical Chemistry

Sulfur specifically inhibits adenylate kinase in assays for creatine kinase

PJ Russell, J Conner and S Sisson

Elemental sulfur is a specific and potent inhibitor of the muscle-type isoenzyme of adenylate kinase (EC 2.7.4.3). We find inhibition by sulfur and by diadenosine pentaphosphate to be similarly potent and specific. Some properties of inhibition of adenylate kinase isoenzymes by sulfur are given. The adenylate kinase isoenzymes from skeletal muscle, brain, and heart muscle are inhibited by sulfur; those from liver and kidney are not. Other enzymes not inhibited by sulfur include the isoenzymes of creatine kinase (EC 2.7.3.2). We show that creatine kinase can be measured in serum when adenylate kinase is inhibited by sulfur, and that the sensitivity and specificity of this inhibition are of the same order as the inhibition of serum adenylate kinase activity by AMP plus diadenosine pentaphosphate.




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Copyright © 1984 by the American Association for Clinical Chemistry.