Abstract
A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants. This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N-glycosylated. The corresponding gene is unique in the carrot genome and induced by cold. The antifreeze protein appears to be localized within the apoplast.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Antifreeze Proteins
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Base Sequence
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Blotting, Western
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Chromatography, Gel
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Chromatography, Ion Exchange
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Cloning, Molecular
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Cold Temperature
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DNA Primers
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Daucus carota / chemistry*
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Electrophoresis, Agar Gel
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Electrophoresis, Polyacrylamide Gel
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Glycoproteins / chemistry
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Glycoproteins / genetics
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Glycoproteins / isolation & purification*
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Glycosylation
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Organelles / chemistry
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / isolation & purification
Substances
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Antifreeze Proteins
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DNA Primers
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Glycoproteins
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Recombinant Proteins