O_2 Binding Properties of Human Serum Albumin Quadruple Mutant Complexed Iron Protoporphyrin IX with Axial His-186 Coordination
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概要
- 論文の詳細を見る
- 2009-08-05
著者
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Komatsu T
Research Institute For Science And Engineering Waseda University
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Komatsu T
Department Of Polymer Chemistry Waseda University
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Komatsu T
Department Of Polymer Chemistry Advanced Research Institute For Science And Engineering Waseda Unive
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Komatsu Teruyuki
Research Institute For Science And Engineering Waseda University
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Komatsu Teruyuki
慶応義塾大学 医学部呼吸器外科
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Tsuchida E
Advanced Research Institute For Science And Engineering Waseda University
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Tsuchida E
Artificial Blood Project Advanced Research Institute For Science And Engineering Waseda University
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Tsuchida E
Advanced Research Institute For Science And Engineering Department Of Polymer Chemistry Waseda Unive
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Tsuchida E
Research Institute For Science And Engineering Waseda University
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Tsuchida E
Waseda Univ. Tokyo Jpn
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Tsuchida Eishun
早稲田大学理工学総合研究センター
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Tsuchida E
Waseda Univ. Tokyo
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Nakagawa Akito
Research Institute For Science And Engineering Waseda University
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TSUCHIDA Eishun
Research Institute for Science and Engineering, Waseda University
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CURRY Stephen
Biophysics Section, Blackett Laboratory, Imperial College London
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Tsuchida Eishun
Research Institute For Science And Engineering Waseda University
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Tsuchida Eishun
Advanced Research Institute For Science And Engineering Waseda University
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Curry Stephen
Biophysics Section Blackett Laboratory Imperial College
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Curry Stephen
Biophysics Section Blackett Laboratory Imperial College London
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Komatsu Teruyuki
Department Of Polymer Chemistry Waseda University
関連論文
- Lessons from the Crystallographic Analysis of Small Molecule Binding to Human Serum Albumin
- O_2 Binding Properties of Human Serum Albumin Quadruple Mutant Complexed Iron Protoporphyrin IX with Axial His-186 Coordination
- Nitrosyl Iron(II)Complex of meso-Tetrakis(α, α, α, α-o-pivalamidophenyl)porphyrin with a Covalently Linked 2-Methylimidazolylalkyl Group
- Virus removal from hemoglobin solution using Planova Membrane
- Carbonylation of oxyhemoglobin solution (HbO_2→HbCO) using a membrane oxygenator
- Characteristics of Bovine Hemoglobin as a Potential Source of Hemoglobin-Vesicles for an Artificial Oxygen Carrier
- Reduction of Methemoglobin via Electron Transfer across the Bilayer Membrane of Hb Vesicles
- Differences in Oxygen Transport and Physical Property between Encapsulated Hemoglobin and Cell-free Hemoglobin
- Coordination Behavior of O_2 and CO in a Solid Film Consisting of Hemoglobin and Maltose
- Cryoprotection of Synthetic Glycolipids for Phospholipid Vesicles