２成分系タンパク質溶液の超遠心沈降特性

DOI Web Site Web Site 被引用文献4件 参考文献8件
  • 入谷 英司
    名古屋大学大学院工学研究科 分子化学工学専攻
  • 赤塚 信也
    名古屋大学大学院工学研究科 分子化学工学専攻 旭硝子 (株)
  • 村瀬 敏朗
    名古屋大学大学院工学研究科 分子化学工学専攻

書誌事項

タイトル別名
  • Sedimentation Behavior of Binary Protein Mixtures in Ultracentrifugation Field.
  • 2セイブンケイ タンパクシツ ヨウエキ ノ チョウ エンシン チンコウ トクセ

この論文をさがす

抄録

The sedimentation rate in ultracentrifugation of an aqueous solution of the mixtures of bovine serum albumin (BSA) and egg white lysozyme has been measured using Schlieren optics in an analytical ultracentrifuge. It was highlighted through this study that the electrical nature of macromolecules plays a significant role in determining the sedimentation behavior in ultracentrifugation of binary protein mixtures. In the pH range where both protein molecules were electropositive, the molecules sedimented independently due to the electrostatic repulsive force acting between BSA and lysozyme molecules. In contrast, in the pH range where two protein molecules had opposite electrical charges, the complex was formed because of the electrostatic attraction between BSA and lysozyme molecules, and it sedimented with a sedimentation rate larger than that for free BSA alone. However, when enough salts were present in the solution, the electrostatic attraction between solutes was reduced due to repression of the electrical double layer, and thus a complex with a large sedimentation rate did not form. This study revealed that the solution environment can have profound effects upon the sedimentation behavior in ultracentrifugation of binary protein mixtures.

収録刊行物

被引用文献 (4)*注記

もっと見る

参考文献 (8)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ