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.
Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota)
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Maggie SMALLWOOD, Dawn WORRALL, Louise BYASS, Luisa ELIAS, David ASHFORD, Charlotte J. DOUCET, Chris HOLT, Julia TELFORD, Peter LILLFORD, Dianna J. BOWLES; Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota). Biochem J 1 June 1999; 340 (2): 385–391. doi: https://doi.org/10.1042/bj3400385
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