Oxygen‐binding property of hemoglobin films

Jooeun Chung, Shinji Takeoka, Hiroyuki Nishide, Eishun Tsuchida*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


Oxygenated and deoxygenated hemoglobin films were obtained by drying corresponding hemoglobin solutions with maltose (≧0.3 M). The resulting hemoglobin films were homogeneous and smooth, and the methemoglobin formation in the oxyhemoglobin film was well suppressed. The dry, rigid networks of maltose molecules work to preserve the conformation of hemoglobin against the removal of water. The coordination of oxygen to the deoxygenated hemoglobin film was slow and saturated up to 50%, while nearly 100% saturation was achieved if the film contained a residual moisture of 8.7%.

Original languageEnglish
Pages (from-to)385-389
Number of pages5
JournalPolymers for Advanced Technologies
Issue number7
Publication statusPublished - 1994 Jul


  • Dehydration
  • Film
  • Hemoglobin
  • Maltose
  • Methemoglobin
  • Oxygen binding

ASJC Scopus subject areas

  • Polymers and Plastics


Dive into the research topics of 'Oxygen‐binding property of hemoglobin films'. Together they form a unique fingerprint.

Cite this