Affordable Access

Publisher Website

Equilibrium and non-equilibrium complexes between bovine serum albumin and dextran sulfate—II. Equilibrium complexes in solution

Authors
Journal
Food Hydrocolloids
0268-005X
Publisher
Elsevier
Publication Date
Volume
2
Issue
4
Identifiers
DOI: 10.1016/s0268-005x(88)80026-2

Abstract

Abstract Equilibrium complexes between bovine serum albumin (BSA) and dextran sulfate (DS) were studied in aqueous solutions at low ionic strength and pHs just above the BSA isoelectric point by viscometry, diffusion and sedimentation velocity methods. Under these conditions the BSA-on-DS sorption is non-cooperative. The intrinsic viscosity of complexes grows linearly with increasing DS weight fraction in the complex, while the diffusion constant remains practically unchanged. Constant-length prolate ellipsoids of revolution with variable axial ratio as well as constant-size Gaussian coils are particles hydrodynamically equivalent to BSA—DS complexes of different compositions.

There are no comments yet on this publication. Be the first to share your thoughts.