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

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.

authors

• Ross, Joseph

published proceedings

• Cryobiology

author list (cited authors)

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

citation count

• 25

complete list of authors

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

publication date

• October 2005

publisher

• Elsevier  Publisher

published in

• Cryobiology  Journal

keywords

• Amino Acid Sequence
• Amino Acids
• Antifreeze Proteins
• Chromatography
• Cryopreservation
• Forsythia
• Molecular Sequence Data
• Plant Bark
• Plant Proteins
• Time Factors

PubMed Central ID

• 16098506

Digital Object Identifier (DOI)

• 10.1016/j.cryobiol.2005.06.005

start page

• 230

end page

• 234

volume

• 51

issue

• 2

URL

• http%3A%2F%2Fdx.doi.org%2F10.1016%2Fj.cryobiol.2005.06.005