Suppression effect of methemoglobin formation in hemoglobin vesicles by coencapsulating methemoglobin and L-tyrosine

Tomoyasu Atoji, Motonari Aihara, Shinji Takeoka, Eishun Tsuchida

Research output: Contribution to conferencePaper

Abstract

Oxyhemoglobin(oxyHb) of Hb-based oxygen carriers reacts with hydrogen peroxide(H 2O 2) to convert metHb and loses its oxygen binding ability. We have developed Hb-vesicles which encapsulate concentrated Hb with phospholipids bilayer membrane. In this study, we constructed a suppression system of metHb formation within Hb-vesicles using the peroxidase activity of metHb with L-Tyr. We could suppress the metHb formation of the oxyHb solution by adding metHb/L-Tyr in the experiment of stepwise addition of H 2O 2. We also confirmed similar effect in Hb vesicles coencapsulating metHb/L-Tyr. Furthermore, it was also effective in vivo. We concluded that H 2O 2 was stably eliminated by the metHb/L-Tyr system in Hb-vesicles, and oxyHb was protected from H 2O 2 reaction.

Original languageEnglish
Number of pages1
Publication statusPublished - 2005 Dec 1
Event54th SPSJ Annual Meeting 2005 - Yokohama, Japan
Duration: 2005 May 252005 May 27

Conference

Conference54th SPSJ Annual Meeting 2005
CountryJapan
CityYokohama
Period05/5/2505/5/27

    Fingerprint

Keywords

  • Hb-vesicles
  • Hydrogen peroxide
  • L-tyrosine
  • MetHb
  • Peroxidase activity

ASJC Scopus subject areas

  • Engineering(all)

Cite this

Atoji, T., Aihara, M., Takeoka, S., & Tsuchida, E. (2005). Suppression effect of methemoglobin formation in hemoglobin vesicles by coencapsulating methemoglobin and L-tyrosine. Paper presented at 54th SPSJ Annual Meeting 2005, Yokohama, Japan.