Skip to main content
Biophysical Journal logoLink to Biophysical Journal
. 1975 Feb;15(2 Pt 1):137–141. doi: 10.1016/s0006-3495(75)85797-3

Hydrodynamic structure of bovine serum albumin determined by transient electric birefringence.

A K Wright, M R Thompson
PMCID: PMC1334600  PMID: 1167468

Abstract

Birefringence relaxation studies on bovine serum albumin (BSA) reveal transient decay described by a double exponential process. The values of the relaxation times lead to estimation of the size of the equivalent ellipsoid of revolution for BSA. Previous measurements of transient birefringence for BSA have shown a single relaxation process, since the apparatus used in obtaining those data was not fast enough to detect the faster relaxation process.

Full text

PDF
137

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Rosseneu-Motreff M. Y., Soetewey F., Lamote R., Peeters H. Dielectric study of the urea denaturation of delipidated and relipidated bovine serum albumin. Biopolymers. 1973 Jun;12(6):1259–1267. doi: 10.1002/bip.1973.360120606. [DOI] [PubMed] [Google Scholar]
  2. Squire P. G., Moser P., O'Konski C. T. The hydrodynamic properties of bovine serum albumin monomer and dimer. Biochemistry. 1968 Dec;7(12):4261–4272. doi: 10.1021/bi00852a018. [DOI] [PubMed] [Google Scholar]
  3. Wright A. K., Duncan R. C., Beekman K. A. A numerical inversion of the perrin equations for rotational diffusion constants for ellipsoids of revolution by iterative techniques. Biophys J. 1973 Aug;13(8):795–803. doi: 10.1016/S0006-3495(73)86025-4. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biophysical Journal are provided here courtesy of The Biophysical Society

RESOURCES