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. 1974 Dec;71(12):4693–4697. doi: 10.1073/pnas.71.12.4693

Sites of Acetylation of Sickle Cell Hemoglobin by Aspirin

Mir Shamsuddin *,†,†, R George Mason *,†,†, James M Ritchey *,†,†, George R Honig *,†,†, Irving M Klotz *,†,†
PMCID: PMC433962  PMID: 4531009

Abstract

Aspirin acetylates a variety of sites on both the α and β chains of hemoglobin S. Nevertheless, the vast majority of acetyl groups become attached to three loci: βLys 59, βLys 144, and αLys 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.

Keywords: acetylsalicylic acid, acetylated lysine residues, α and β chains, chromatographic fractionation, radioactive label

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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