Structural specificities in acylation of hemoglobin and sickle hemoglobin by diaspirins

L. E. Wood, D. N. Haney, J. R. Patel, S. E. Clare, G. Y. Shi, L. C. King, I. M. Klotz

Research output: Contribution to journalArticlepeer-review

22 Scopus citations

Abstract

Double-headed aspirins with bridging groups of different length and molecular structure have been examined for their reactivity with hemoglobin A or S. The compounds constructed are bound in the β-cleft and show a wide range of β-β cross-linking effectiveness. Oxygenation curves of the modified hemoglobins in the presence of inositol hexaphosphate are strikingly modified. Many of the diaspirins also produce substantial changes in the minimum gelling concentration of sickle hemoglobin. These reagents offer possibilities for further enhancement of specificity toward hemoglobin, particularly by taking advatage of stereoselectivities.

Original languageEnglish (US)
Pages (from-to)7046-7052
Number of pages7
JournalJournal of Biological Chemistry
Volume256
Issue number13
StatePublished - 1981

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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