Oxygen-binding property of hemoglobin films

Jooeun Chung, Shinji Takeoka, Hiroyuki Nishide, Eishun Tsuchida

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Oxygenated and deoxygenated hemoglobin films were obtained by drying corresponding hemoglobin solutions with maltose (qq0.3 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
Volume5
Issue number7
DOIs
Publication statusPublished - 1994 Jul

Fingerprint

Hemoglobin
Hemoglobins
Oxygen
Maltose
Methemoglobin
Oxyhemoglobins
Conformations
Drying
Moisture
Molecules
Water

ASJC Scopus subject areas

  • Polymers and Plastics

Cite this

Oxygen-binding property of hemoglobin films. / Chung, Jooeun; Takeoka, Shinji; Nishide, Hiroyuki; Tsuchida, Eishun.

In: Polymers for Advanced Technologies, Vol. 5, No. 7, 07.1994, p. 385-389.

Research output: Contribution to journalArticle

Chung, Jooeun ; Takeoka, Shinji ; Nishide, Hiroyuki ; Tsuchida, Eishun. / Oxygen-binding property of hemoglobin films. In: Polymers for Advanced Technologies. 1994 ; Vol. 5, No. 7. pp. 385-389.
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