Gallez B, De Keyser JL, Debuyst R, Dejehet F, Neuvens L, Dumont P
Department of Pharmaceutical Sciences, Catholic University of Louvain, Brussels, Belgium.
The ability of a nitroxyl fatty acid (NFA) to bind specifically to albumin
is abolished when, in the absence of stabilizers, a 4% solution of this
protein is heated above a critical temperature of 60 degrees C. This treatment
leads to the formation of "albumin polymers" as classically evidenced by
GPC. Since the bound fraction is evidenced in EPR spectroscopy by a large
anisotropic component, the presence of this anisotropy can be used in the
assessment of the quality of the pharmaceutical preparations of albumin,
which are usually pasteurized in order to inactivate viruses. Moreover,
in sharp contrast with the behavior of albumin dispersions, lyophilised
albumin subjected to heat treatment at 70 degrees C for 24 h left the protein
untouched regarding its NFA binding and GPC profile.
PMID: 8788128, UI: 96380115