Sites of Acetylation of Sickle Cell Hemoglobin by Aspirin

Abstract

Aspirin acetylates a variety of sites on both the alpha and beta chains of hemoglobin S. Nevertheless, the vast majority of acetyl groups become attached to three loci: betaLys 59, betaLys 144, and alphaLys 90. These observations reveal some molecular details of this transacylation reaction and suggest interesting possibilities for its extension to other acylsalicylates with a variety of different structures.