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

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

doi:10.1016/j.cryobiol.2005.06.005

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

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

CNAP

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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 0.5 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.

Original language	English
Pages (from-to)	230-234
Number of pages	5
Journal	Cryobiology
Volume	51
Issue number	2
DOIs	https://doi.org/10.1016/j.cryobiol.2005.06.005
Publication status	Published - Oct 2005

Keywords

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

Access to Document

10.1016/j.cryobiol.2005.06.005

Cite this

@article{06bdd74621da4030b2a690648bdc4d65,

title = "Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.)",

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 0.5 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.",

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

author = "Simpson, {D J} and M Smallwood and S Twigg and Doucet, {C J} and J Ross and Bowles, {D J}",

year = "2005",

month = oct,

doi = "10.1016/j.cryobiol.2005.06.005",

language = "English",

volume = "51",

pages = "230--234",

journal = "Cryobiology",

issn = "0011-2240",

publisher = "Academic Press",

number = "2",

}

TY - JOUR

T1 - Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.)

AU - Simpson, D J

AU - Smallwood, M

AU - Twigg, S

AU - Doucet, C J

AU - Ross, J

AU - Bowles, D J

PY - 2005/10

Y1 - 2005/10

N2 - 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.

AB - 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.

KW - antifreeze protein

KW - dehydrin

KW - Forsythia suspensa

KW - Y-segment

KW - purification

KW - cold-acclimated

KW - recrystallization inhibition

KW - bark

KW - heat-stability

KW - chromatography

KW - LOW-TEMPERATURE

KW - PLANTS

U2 - 10.1016/j.cryobiol.2005.06.005

DO - 10.1016/j.cryobiol.2005.06.005

M3 - Article

SN - 0011-2240

VL - 51

SP - 230

EP - 234

JO - Cryobiology

JF - Cryobiology

IS - 2

ER -