Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.). Academic Article uri icon


  • 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.

author list (cited authors)

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

complete list of authors

  • Simpson, Deborah J||Smallwood, Maggie||Twigg, Sarah||Doucet, Charlotte J||Ross, Joe||Bowles, Dianna J

publication date

  • January 1, 2005 11:11 AM