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. Here, 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 in the Hb vesicles by coencapsulating metHb and L-Tyr on the experiment of stepwise addition of H 2O 2 and autoxidation condition. Furthermore, this system was also effective in vivo. We concluded that H 2O 2 was effectively eliminated by the metHb/L-Tyr system in the Hb vesicles, and oxygen carrying ability was successfully prolonged.
Original language | English |
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Pages | 4927-4928 |
Number of pages | 2 |
Publication status | Published - 2005 Dec 1 |
Event | 54th SPSJ Symposium on Macromolecules - Yamagata, Japan Duration: 2005 Sept 20 → 2005 Sept 22 |
Other
Other | 54th SPSJ Symposium on Macromolecules |
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Country/Territory | Japan |
City | Yamagata |
Period | 05/9/20 → 05/9/22 |
Keywords
- Hb vesicles
- Hydrogen peroxide/
- L-tyrosine
- MetHb
- Peroxidase activity
ASJC Scopus subject areas
- Engineering(all)