Related Experiment Video
Updated: Jun 28, 2026
Detection of Abnormal Prion Protein by Immunohistochemistry
Published on: May 5, 2023
Ablation of prion protein immunoreactivity by heating in saturated calcium hydroxide
Justin J Greenlee1, Eric M Nicholson, Amir N Hamir
1Virus and Prion Diseases of Livestock Research Unit, National Animal Disease Center, USDA, Agricultural Research Service, 2300 Dayton Avenue, Ames, IA, USA, 50010. justin.greenlee@ars.usda.gov
Background:
Prions, the infectious agents that cause transmissible spongiform encephalopathies (TSEs), are relatively resistant to destruction by physical, enzymatic, and chemical treatments. Hydrolysis in boiling saturated calcium hydroxide (limewater) utilizes inexpensive chemicals to digest protein components of offal. The purpose of this work was to determine if incubating brain material from scrapie-infected sheep in near-boiling saturated calcium hydroxide solution (Ca(OH)2) would abolish immunoreactivity of the infectious prion (PrPSc) as determined by western blot.
Findings:
After incubating for as few as 10 minutes in saturated calcium hydroxide at 99 degrees C, immunoreactivity of protease resistant bands by western blot analysis is completely lost.
Conclusion:
Boiling in limewater may offer an alternative for disposal of carcasses and enable alternative uses for rendered products from potentially infected carcasses.
