Tritiated Digoxin Binding to (Na + + K + )-Activated Adenosine Triphosphatase: Possible Allosteric Site

作者：Arnold Schwartz, Hideo Matsui, Arline H. Laughter · 发表于：Science · 年份：1968 · DOI：10.1126/science.160.3825.323 · 被引用次数：175 · 研究领域：Enzyme function and inhibition、Chemical Reactions and Isotopes、Ion channel regulation and function

Tritiated H(3)-digoxin specifically binds to a cardiac (Na(+) + K(+))-activated adenosine triphosphatase. In the presence of adenosine triphosphate and other nucleoside di- and triphosphates, binding is stimulated by sodium ion, the apparent rate constant being similar to that reported for phosphorus-32 incorporation from adenosine triphosphate and for the adenosine triphosphatase activity. In the presence of magnesium, manganese, inorganic phosphate, or other ions, sodium ion inhibits binding. The data support an allosteric type of sodium-potassium ion pump.