Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.) |
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Authors: | Simpson Deborah J Smallwood Maggie Twigg Sarah Doucet Charlotte J Ross Joe Bowles Dianna J |
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Institution: | Cardiff School of Biosciences, Main Building, Cardiff University, Museum Avenue, Cardiff CF10 3TL, UK. simpsondj@cardiff.ac.uk |
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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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Keywords: | Antifreeze protein Dehydrin Forsythia suspensa Y-segment Purification Cold-acclimated Recrystallization inhibition Bark Heat-stability Chromatography |
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