The interaction of deoxyhemoglobin with the red cell membrane

Nurith Shaklai*, Hana Abrahami

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The interaction of deoxyhemoglobin with the red cell membrane is characterized by comparing the affinity of deoxyhemoglobin for the membrane with that of oxyhemoglobin. The two techniques used, namely light scattering induced changes and quenching of the fluorescence intensity of a membrane embedded probe, demonstrate that deoxyhemoglobin exhibits a much lower affinity for the membrane than that of oxyhemoglobin. The binding constant of 2×10 M−1 calculated for deoxyhemoglobin at 5 mM phosphate buffer and pH=6.0 is two orders of magnitude lower than the one calculated for oxyhemoglobin. It is estimated that under physiological conditions the only species capable of interacting with the membrane is the oxyhemoglobin.

Original languageEnglish
Pages (from-to)1105-1112
Number of pages8
JournalTopics in Catalysis
Volume95
Issue number3
DOIs
StatePublished - 1980

Keywords

  • AS
  • Carbomonoxyhemoglobin
  • Deoxy-Hb
  • Hb
  • HbCO
  • HbO
  • anthroyl stearic acid
  • deoxyhemoglobin
  • hemoglobin
  • oxyhemoglobin

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