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. 1999 Jun 1;340(Pt 2):385–391.

Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota).

M Smallwood 1, D Worrall 1, L Byass 1, L Elias 1, D Ashford 1, C J Doucet 1, C Holt 1, J Telford 1, P Lillford 1, D J Bowles 1
PMCID: PMC1220261  PMID: 10333479

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.

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Selected References

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