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  • Title: Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.).
    Author: Simpson DJ, Smallwood M, Twigg S, Doucet CJ, Ross J, Bowles DJ.
    Journal: Cryobiology; 2005 Oct; 51(2):230-4. PubMed ID: 16098506.
    Abstract:
    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 0.5microg pure protein obtained from 35 g bark. RI activity is seen with as little as 6 microg ml(-1) protein. Sequence homology was seen with dehydrins, and forsythia AFP contains the Y-segment, a conserved region found in many dehydrins.
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