Sites of acetylation of sickle cell hemoglobin by aspirin.
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.
D001241:Aspirin / Q000378:metabolism*; D001665:Binding Sites; D002250:Carbon Radioisotopes; D002852:Chromatography, Ion Exchange; D006451:Hemoglobin, Sickle / Q000378:metabolism*; D006455:Hemoglobins, Abnormal / Q000378:metabolism*; D006868:Hydrolysis; D008961:Models, Structural; D010455:Peptides / Q000378:metabolism; D011487:Protein Conformation; D014357:Trypsin
D002250:Carbon Radioisotopes; D006451:Hemoglobin, Sickle; D006455:Hemoglobins, Abnormal; D010455:Peptides; D014357:Trypsin; D001241:Aspirin