PMID: 6408963Jul 1, 1983Paper

Thermal denaturation of alpha 1-protease inhibitor. Stabilization by neutral salts and sugars

The American Review of Respiratory Disease
C B GlaserA Childs

Abstract

Alpha 1-protease inhibitor (alpha 1 PI), also called alpha 1-antitrypsin, may be useful for replacement therapy in a number of chronic or acute disorders. The risk associated with the possible presence of hepatitis virus can be greatly reduced by pasteurization at 60 degrees C for 10 h. A series of thermal denaturation profiles was obtained in the presence of various protein stabilizers using the increase in 1,8-anilinonaphthalene sulfonate fluorescence that accompanies protein denaturation. A parallel series of experiments was conducted to evaluate each additive for its capacity to protect the biological activity of alpha 1 PI. As much as 92% of the inhibitory activity against elastase and trypsin could be recovered after pasteurization in buffer containing citrate (1.2 M) and either EDTA (0.5 M) or gluconate (1.2 M). Loss of activity was not affected by protein concentration. In conclusion, conditions have been developed to protect the bulk of alpha 1 PI from denaturation during pasteurization, and this should give an added impetus to efforts to test the efficacy of this protein in various clinical conditions.

Citations

Nov 1, 1985·Hepatology : Official Journal of the American Association for the Study of Liver Diseases·R H PurcellM E Hrinda
Jan 1, 1984·Vox Sanguinis·C WilliamsK C Ingham
Apr 13, 2004·Journal of Applied Physiology·Shawn E Soutiere, Wayne Mitzner
Aug 24, 2000·Journal of Applied Physiology·R F GomesJ H Bates
Mar 10, 2001·Magnetic Resonance in Medicine : Official Journal of the Society of Magnetic Resonance in Medicine·H E MöllerG A Johnson
Dec 22, 1999·Journal of Applied Physiology·R Tanaka, M S Ludwig
Jun 1, 1997·Analytical Biochemistry·M Gauthier, P A Patston

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