he "free" NO consumed by hemoglobin is also released and exhaled. Then, the oxygenation process is repeated.

"Once, we thought the primary job of hemoglobin was to carry oxygen," said co-author Joseph Bonaventura in an interview. "Now we can show that nitric oxide delivery may be comparable in importance. Here we have the lungs synthesizing a compound and delivering it to tissue where it is metabolized, just as oxygen is."

In addition, the research shows that NO has a regulatory "allosteric" function that has not been described before, Stamler said. Allosteric regulation is when one molecule causes a protein to change its shape and, thereby, its function. Hemoglobin is "a classic allosteric protein" because its function depends on whether or not oxygen is bound to it,Stamler said. Now, the Duke researchers said, NO is also involved in the allosteric transition of hemoglobin.

'"/>

Contact: Renee Twombly
twomb001@mc.duke.edu
919-660-1313
Duke University
29-Apr-1996

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