Preferential solvent binding and change in conformation of bovine serum albumin in 2-chloroethanol–water mixed solvents
✍ Scribed by Eddie Maes
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1976
- Tongue
- English
- Weight
- 382 KB
- Volume
- 15
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Solvent binding to bovine serum albumin in 2‐chloroethanol‐water mixed solvents of different composition, measured previously by Inoue and Timasheff (Biopolymers (1972) 11, 737–43) is applied to a hydrodynamic study of the solvated protein.
From sedimentation and diffusion data, the apparent molecular weight of the solvated protein particle can be calculated, provided an average partial specific volume, computed from the composition of the particle, is introduced in Svedberg's equation. The unsolvated molecular weight of the protein can than be calculated by subtraction of the bound solvent. Further data on the hydrodynamic particle (f/f~min~ and axial ratio of the equivalent ellipsoid) are readily calculated from these experiments, and reinforce the supposition that 2‐chloroethanol is a strong helix‐inducing solvent.