Related Experiment Video
Updated: Sep 20, 2026

Sedimentation Equilibrium of a Small Oligomer-forming Membrane Protein: Effect of Histidine Protonation on Pentameric Stability
Published on: April 2, 2015
Behavior of S1- and S2-ovalbumin and S-ovalbumin A1 in urea solution: kinetics and equilibria
Hugh A McKenzie1, Robert D Frier
1School of Chemistry, University College, University of New South Wales, Australian Defence Force Academy, Canberra, Australia ACT 2600. h.mckenzie@adfa.edu.au
Abstract:
The isolation of S-, S1-, and S2-ovalbumin from domestic hen egg R-ovalbumin and of two methods for S-ovalbumin A1 are described. The first is by heat treatment of R-ovalbumin A1 and the second is of R-ovalbumin followed by fractionation on Sepharose. A kinetics and equilibrium study is made of their behavior in the presence of urea and compared with that of R-ovalbumins. As anticipated, the S-ovalbumins are much more resistant to urea than R-ovalbumins. Unlike the latter, S-ovalbumins' equilibrium profiles have a simpler sigmoidal shape. The unfolding of S1- and S2-ovalbumin is an order of magnitude slower than that of R-ovalbumin. Some possible structural differences between R- and S-ovalbumin forms and their significance are discussed.
Related Concept Videos
Position of Equilibrium in Acid-Base Reactions
Two-Compartment Open Model: IV Bolus Administration
The disparity between drug input and the sum of drug transfer rates between...
Multi-Step Reactions
Compartment Models: Two-Compartment Model
Nonlinear Pharmacokinetics: Bioavailability and Protein-Drug Binding
To quantify the extent of bioavailability, pharmacologists often use a parameter called .
One-Compartment Open Model for IV Bolus Administration: Estimation of Elimination Rate Constant, Half-Life and Volume of Distribution
