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

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Published
  • M Smallwood
  • D Worrall
  • L Byass
  • L Elias
  • D Ashford
  • C J Doucet
  • C Holt
  • J Telford
  • P Lillford
  • D J Bowles
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<mark>Journal publication date</mark>1/06/1999
<mark>Journal</mark>Biochemical Journal
Issue number2
Volume340
Number of pages7
Pages (from-to)385-391
Publication StatusPublished
<mark>Original language</mark>English

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.