Prolonged oxygen-carrying ability of hemoglobin vesicles by coencapsulation of catalase in vivo.
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 (H(2)O(2)), in vivo in addition to autoxidation. We focused on the enzymatic elimination of H(2)O(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 10(4) 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.
Teramura
Yuji
Y
Advanced Research Institute for Science and Engineering, Waseda University, Tokyo 169-8555, Japan.
Kanazawa
Hideo
H
Sakai
Hiromi
H
Takeoka
Shinji
S
Tsuchida
Eishun
E
D000818:Animals; D002374:Catalase / Q000737:chemistry / Q000378:metabolism*; D004337:Drug Carriers; D006454:Hemoglobins / Q000378:metabolism*; D006801:Humans; D006861:Hydrogen Peroxide / Q000737:chemistry; D008070:Lipopolysaccharides / Q000737:chemistry; D008706:Methemoglobin / Q000096:biosynthesis; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar
D004337:Drug Carriers; D006454:Hemoglobins; D008070:Lipopolysaccharides; D008706:Methemoglobin; D006861:Hydrogen Peroxide; D002374:Catalase; D010100:Oxygen