Prolonged Oxygen-Carrying Ability of Hemoglobin Vesicles by Coencapsulation of Catalase in Vivo

Yuji Teramura; Hideo Kanazawa; Hiromi Sakai; Shinji Takeoka; Eishun Tsuchida

doi:10.1021/bc0340619

Prolonged Oxygen-Carrying Ability of Hemoglobin Vesicles by Coencapsulation of Catalase in Vivo

Yuji Teramura, Hideo Kanazawa, Hiromi Sakai, Shinji Takeoka, Eishun Tsuchida^*

^*Corresponding author for this work

School of Advanced Science and Engineering

Research output: Contribution to journal › Article › peer-review

34 Citations (Scopus)

Abstract

Hemoglobin (Hb) vesicles (particle diameter, ca. 250 nm) have been developed as Hb-based oxygen carriers in which a purified Hb solution is encapsulated with a phospholipid bilayer membrane. The oxidation of Hb to nonfunctional ferric Hb (metHb) was caused by reactive oxygen species, especially hydrogen peroxide (H₂O₂), in vivo in addition to autoxidation. We focused on the enzymatic elimination of H₂O ₂ to suppress the metHb formation in the Hb vesicles. In this study, we coencapsulated catalase with Hb within vesicles and studied the rate of metHb formation in vivo. The Hb vesicles containing 5.6 x 10⁴ unit mL^-1 catalase decreased the rate of metHb formation by half in comparison with Hb vesicles without catalase. We succeeded in prolonging the oxygen-carrying ability of the Hb vesicle in vivo by the coencapsulation of catalase.

Original language	English
Pages (from-to)	1171-1176
Number of pages	6
Journal	Bioconjugate Chemistry
Volume	14
Issue number	6
DOIs	https://doi.org/10.1021/bc0340619
Publication status	Published - 2003

ASJC Scopus subject areas

Biotechnology
Bioengineering
Biomedical Engineering
Pharmacology
Pharmaceutical Science
Organic Chemistry

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abstract = "Hemoglobin (Hb) vesicles (particle diameter, ca. 250 nm) have been developed as Hb-based oxygen carriers in which a purified Hb solution is encapsulated with a phospholipid bilayer membrane. The oxidation of Hb to nonfunctional ferric Hb (metHb) was caused by reactive oxygen species, especially hydrogen peroxide (H2O2), in vivo in addition to autoxidation. We focused on the enzymatic elimination of H2O 2 to suppress the metHb formation in the Hb vesicles. In this study, we coencapsulated catalase with Hb within vesicles and studied the rate of metHb formation in vivo. The Hb vesicles containing 5.6 x 104 unit mL-1 catalase decreased the rate of metHb formation by half in comparison with Hb vesicles without catalase. We succeeded in prolonging the oxygen-carrying ability of the Hb vesicle in vivo by the coencapsulation of catalase.",

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T1 - Prolonged Oxygen-Carrying Ability of Hemoglobin Vesicles by Coencapsulation of Catalase in Vivo

AU - Teramura, Yuji

AU - Kanazawa, Hideo

AU - Sakai, Hiromi

AU - Takeoka, Shinji

AU - Tsuchida, Eishun

PY - 2003

Y1 - 2003

N2 - Hemoglobin (Hb) vesicles (particle diameter, ca. 250 nm) have been developed as Hb-based oxygen carriers in which a purified Hb solution is encapsulated with a phospholipid bilayer membrane. The oxidation of Hb to nonfunctional ferric Hb (metHb) was caused by reactive oxygen species, especially hydrogen peroxide (H2O2), in vivo in addition to autoxidation. We focused on the enzymatic elimination of H2O 2 to suppress the metHb formation in the Hb vesicles. In this study, we coencapsulated catalase with Hb within vesicles and studied the rate of metHb formation in vivo. The Hb vesicles containing 5.6 x 104 unit mL-1 catalase decreased the rate of metHb formation by half in comparison with Hb vesicles without catalase. We succeeded in prolonging the oxygen-carrying ability of the Hb vesicle in vivo by the coencapsulation of catalase.

AB - Hemoglobin (Hb) vesicles (particle diameter, ca. 250 nm) have been developed as Hb-based oxygen carriers in which a purified Hb solution is encapsulated with a phospholipid bilayer membrane. The oxidation of Hb to nonfunctional ferric Hb (metHb) was caused by reactive oxygen species, especially hydrogen peroxide (H2O2), in vivo in addition to autoxidation. We focused on the enzymatic elimination of H2O 2 to suppress the metHb formation in the Hb vesicles. In this study, we coencapsulated catalase with Hb within vesicles and studied the rate of metHb formation in vivo. The Hb vesicles containing 5.6 x 104 unit mL-1 catalase decreased the rate of metHb formation by half in comparison with Hb vesicles without catalase. We succeeded in prolonging the oxygen-carrying ability of the Hb vesicle in vivo by the coencapsulation of catalase.

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Prolonged Oxygen-Carrying Ability of Hemoglobin Vesicles by Coencapsulation of Catalase in Vivo

Abstract

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