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Updated: Aug 8, 2026

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Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification
Published on: May 5, 2017
Antifreeze protein produced endogenously in winter rye leaves
1Department of Biology, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada.
Plant Physiology
|October 1, 1992
Summary
Cold-acclimated winter rye produces its own antifreeze protein. This protein, found in leaf apoplast, protects plants by altering ice crystal growth and lowering water
Area of Science:
- Plant Biology
- Biochemistry
- Cryobiology
Background:
- Winter rye (Secale cereale L.) exhibits remarkable frost tolerance after cold acclimation.
- Extracellular ice formation is a critical factor influencing plant survival at freezing temperatures.
Purpose of the Study:
- To investigate the presence and function of endogenous antifreeze proteins in cold-acclimated winter rye.
- To characterize the properties of the identified antifreeze protein.
Main Methods:
- Cold acclimation of winter rye plants.
- Extraction of proteins from the apoplast of winter rye leaves.
- Partial purification and characterization of the extracted protein.
- Assay of ice-binding and ice-nucleating activity.
Main Results:
- Antifreeze protein was identified in the apoplast of cold-acclimated winter rye leaves.
- The purified protein demonstrated the ability to modify ice crystal morphology.
- The protein noncolligatively depressed the freezing point of water, confirming its antifreeze activity.
Conclusions:
- Cold-acclimated winter rye possesses endogenously produced antifreeze proteins.
- These proteins play a crucial role in protecting winter rye from freezing damage by regulating extracellular ice formation.
- The findings contribute to understanding plant cryoprotective mechanisms.
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