Sites of acetylation of sickle cell hemoglobin by aspirin
- PMID: 4531009
- PMCID: PMC433962
- DOI: 10.1073/pnas.71.12.4693
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.
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