The effects of pasteurisation on albumin: an EPR binding assay for polymeric albumin.
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.
Gallez
B
B
Department of Pharmaceutical Sciences, Catholic University of Louvain, Brussels, Belgium.
De Keyser
J L
JL
Debuyst
R
R
Dejehet
F
F
Neuvens
L
L
Dumont
P
P
D002850:Chromatography, Gel; D003497:Cyclic N-Oxides / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D005612:Freeze Drying; D006358:Hot Temperature; D006801:Humans; D007850:Lauric Acids / Q000737:chemistry; D011108:Polymers; D011485:Protein Binding; D012709:Serum Albumin / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry; D013113:Spin Labels; D013242:Sterilization
D003497:Cyclic N-Oxides; D007850:Lauric Acids; D011108:Polymers; D012709:Serum Albumin; D013113:Spin Labels; C084843:12-(2,2,5,5-tetramethyl-1-pyrrolidinoxyl-3-carbonylamino)dodecanoate; D012710:Serum Albumin, Bovine