Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.)

D J Simpson, M Smallwood, S Twigg, C J Doucet, J Ross, D J Bowles

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Recrystallisation inhibition (RI) activity has been isolated from cold-acclimated Forsythia suspensa bark and leaves, which is stable when boiled, and not sensitive to reducing agents. The antifreeze activity has been purified to a single 20 kDa protein, using anion exchange, hydroxyapatite chromatography, and gel filtration. The protein is abundant in forsythia bark with 0.5 mu g pure protein obtained from 35 g bark. RI activity is seen with as little as 6 mu g ml(-1) protein. Sequence homology was seen with dehydrins, and forsythia AFP contains the Y-segment, a conserved region found in many dehydrins. (c) 2005 Elsevier Inc. All rights reserved.

Original languageEnglish
Pages (from-to)230-234
Number of pages5
Issue number2
Publication statusPublished - Oct 2005


  • antifreeze protein
  • dehydrin
  • Forsythia suspensa
  • Y-segment
  • purification
  • cold-acclimated
  • recrystallization inhibition
  • bark
  • heat-stability
  • chromatography

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