Sedimentation Behavior of Binary Protein Mixtures in Ultracentrifugation Field.

DOI Web Site Web Site 4 Citations 8 References

Bibliographic Information

Other Title
  • ２成分系タンパク質溶液の超遠心沈降特性
  • 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

Search this article

Abstract

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.

Journal

Citations (4)*help

See more

References(8)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top