通过在体内共包裹过氧化氢酶延长血红蛋白囊泡的携氧能力。

Prolonged oxygen-carrying ability of hemoglobin vesicles by coencapsulation of catalase in vivo.

作者信息

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

机构信息

Advanced Research Institute for Science and Engineering, Waseda University, Tokyo 169-8555, Japan.

出版信息

Bioconjug Chem. 2003 Nov-Dec;14(6):1171-6. doi: 10.1021/bc0340619.

DOI:10.1021/bc0340619

PMID:14624631

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 (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.

摘要

血红蛋白（Hb）囊泡（粒径约250纳米）已被开发为基于血红蛋白的氧载体，其中纯化的血红蛋白溶液被包裹在磷脂双分子层膜中。除了自身氧化外，体内活性氧，尤其是过氧化氢（H₂O₂）会导致Hb氧化为无功能的高铁血红蛋白（metHb）。我们专注于通过酶促消除H₂O₂来抑制Hb囊泡中metHb的形成。在本研究中，我们将过氧化氢酶与Hb共包裹在囊泡中，并研究了体内metHb的形成速率。与不含过氧化氢酶的Hb囊泡相比，含有5.6×10⁴单位·mL⁻¹过氧化氢酶的Hb囊泡使metHb的形成速率降低了一半。通过共包裹过氧化氢酶，我们成功地延长了Hb囊泡在体内的携氧能力。