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Thermal Stability of Human Immunoglobulins with Sorbitol: A Critical Evaluation
Author(s) -
González Martin,
Murature Domingo A.,
Fidelio Gerardo D.
Publication year - 1995
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1995.tb02535.x
Subject(s) - sorbitol , differential scanning calorimetry , chemistry , denaturation (fissile materials) , chromatography , turbidity , thermal stability , dimer , biochemistry , nuclear chemistry , organic chemistry , biology , ecology , physics , thermodynamics
The effect of the additive sorbitol on the thermal stabilization of human IgG was investigated by differential scanning calorimetry and size exclusion chromatography. In the presence of 33% sorbitol, the temperature at which denaturation of IgG began (T i ) was increased from 52 to 65°C. Similarly, the temperature of the maximum heat capacity (T max ) was increased from 69 to 76°C. Sorbitol also decreased dimer aggregation and the extent of oligomerization during heating compared with IgG dissolved in phosphate buffer. Sorbitol at 33% prevented massive protein denaturation but a 10–15% of oligomerization of high molecular weight aggregates with turbidity could not be avoided when heating for 10 h at 60°C. The use of sorbitol 33% to avoid heat denaturation of human IgG during viral inactivation did not prevent protein aggregation or the appearance of turbidity. Consequently, further processing will be required to achieve a product suitable for pharmaceutical use.