By the same authors

From the same journal

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

Research output: Contribution to journalArticlepeer-review

Published copy (DOI)


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


Publication details

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


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.

    Research areas

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

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