Harrington John P, Kobayashi Shiho, Dorman Scott C, Zito Samantha L, Hirsch Rhoda Elison
Department of Chemistry, State University of New York, New Paltz, NY 12561, USA.
Artif Cells Blood Substit Immobil Biotechnol. 2007;35(1):53-67. doi: 10.1080/10731190600974491.
Natural acellular polymeric hemoglobins (Hb) provide oxygen transport and delivery within many terrestrial and marine invertebrate organisms. It has been our premise that these natural acellular Hbs may serve as models of therapeutic hemoglobin-based oxygen carriers (HBOC). Our attention has focused on the acellular Hb from the terrestrial invertebrate, Lumbricus terrestris (Lt), which possesses a unique hierarchical structure and a unique ability to function extracellularly without oxidative damage. Lumbricus Hb and Arenicola Hb are resistant to autoxidation, chemical oxidation by potassium ferricyanide, and have little or no capacity to transfer electrons to Fe(+3)-complexes at 37 degrees C. An understanding of how these invertebrate acellular oxygen carriers maintain their structural integrity and redox stability in vivo is vital for the design of a safe and effective red cell substitute. We report here a positive redox potential for these giant hemoglobins that may lie at the basis for its resistance to oxidation.
天然无细胞聚合血红蛋白（Hb）在许多陆生和海洋无脊椎动物体内提供氧气运输和输送。我们的前提是，这些天然无细胞血红蛋白可作为基于血红蛋白的治疗性氧载体（HBOC）的模型。我们的注意力集中在陆生无脊椎动物蚯蚓（Lumbricus terrestris，Lt）的无细胞血红蛋白上，它具有独特的层次结构和在细胞外发挥功能而无氧化损伤的独特能力。蚯蚓血红蛋白和沙蠋血红蛋白对自氧化、铁氰化钾的化学氧化具有抗性，并且在37℃时几乎没有或没有将电子转移到Fe(+3)络合物的能力。了解这些无脊椎动物无细胞氧载体如何在体内维持其结构完整性和氧化还原稳定性对于设计安全有效的红细胞替代物至关重要。我们在此报告这些巨型血红蛋白的正氧化还原电位，这可能是其抗氧化的基础。
