Inhibition of deoxyhemoglobin S polymerization by glyceraldehyde

A. Seetharama Acharya, Leslie G. Sussman, Wanda M. Jones, James M. Manning

Research output: Contribution to journalArticle

4 Scopus citations


Glyceraldehyde reacts with hemoglobin S in the intact erythrocyte to reduce the degree of polymerization, thereby inhibiting sickling of the erythrocyte. Only five of the 24 amino groups per αβ dimer react with glyceraldehyde; the adducts are present as ketoamine structures, formed by Amadori rearrangement of the initial Schiff base adducts on the protein. The reactive amino groups are the ε{lunate}-amino group of Lys-16 of the α-chain, and the α-amino group of Val-1 as well as the ε{lunate}-amino groups Lys-82, Lys-59, and Lys-120 of the β-chain. Hybrid tetramers were prepared with the modification only on Lys-16 of the α-chain or on the reactive lysine residues of the β-chain. The former derivative gels at a much higher hemoglobin concentration (23 g/dl) than either the latter derivative (16 g/dl) or unmodified deoxyhemoglobin S (15 g/dl). Thus, the modification at Lys-16 of the α-chain is a major factor in the inhibition of sickling by glyceraldehyde.

Original languageEnglish (US)
Pages (from-to)101-109
Number of pages9
JournalAnalytical Biochemistry
Issue number1
StatePublished - Jan 1984

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Acharya, A. S., Sussman, L. G., Jones, W. M., & Manning, J. M. (1984). Inhibition of deoxyhemoglobin S polymerization by glyceraldehyde. Analytical Biochemistry, 136(1), 101-109.