Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota)

M Smallwood; D Worrall; L Byass; L Elias; D Ashford; C J Doucet; C Holt; J Telford; P Lillford; D J Bowles

Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota)

M Smallwood, D Worrall, L Byass, L Elias, D Ashford, C J Doucet, C Holt, J Telford, P Lillford, D J Bowles

CNAP

Research output: Contribution to journal › Article › peer-review

Abstract

A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants, This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N- glycosylated, The corresponding gene is unique in the carrot genome and induced by cold, The antifreeze protein appears to be localized within the apoplast.

Original language	English
Pages (from-to)	385-391
Number of pages	7
Journal	Biochemical journal
Volume	340
Publication status	Published - 1 Jun 1999

Keywords

apoplast
cold-on-regulated gene
ice recrystallization inhibition
polygalacturonase inhibitor protein
thermal hysteresis
THERMAL HYSTERESIS PROTEIN
N-LINKED OLIGOSACCHARIDES
ICE RECRYSTALLIZATION
WINTER RYE
PLANT
SEQUENCE

Cite this

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title = "Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota)",

abstract = "A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants, This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N- glycosylated, The corresponding gene is unique in the carrot genome and induced by cold, The antifreeze protein appears to be localized within the apoplast.",

keywords = "apoplast, cold-on-regulated gene, ice recrystallization inhibition, polygalacturonase inhibitor protein, thermal hysteresis, THERMAL HYSTERESIS PROTEIN, N-LINKED OLIGOSACCHARIDES, ICE RECRYSTALLIZATION, WINTER RYE, PLANT, SEQUENCE",

author = "M Smallwood and D Worrall and L Byass and L Elias and D Ashford and Doucet, {C J} and C Holt and J Telford and P Lillford and Bowles, {D J}",

year = "1999",

month = jun,

day = "1",

language = "English",

volume = "340",

pages = "385--391",

journal = "Biochemical journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

}

TY - JOUR

T1 - Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota)

AU - Smallwood, M

AU - Worrall, D

AU - Byass, L

AU - Elias, L

AU - Ashford, D

AU - Doucet, C J

AU - Holt, C

AU - Telford, J

AU - Lillford, P

AU - Bowles, D J

PY - 1999/6/1

Y1 - 1999/6/1

N2 - A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants, This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N- glycosylated, The corresponding gene is unique in the carrot genome and induced by cold, The antifreeze protein appears to be localized within the apoplast.

AB - A modified assay for inhibition of ice recrystallization which allows unequivocal identification of activity in plant extracts is described. Using this assay a novel, cold-induced, 36 kDa antifreeze protein has been isolated from the tap root of cold-acclimated carrot (Daucus carota) plants, This protein inhibits the recrystallization of ice and exhibits thermal-hysteresis activity. The polypeptide behaves as monomer in solution and is N- glycosylated, The corresponding gene is unique in the carrot genome and induced by cold, The antifreeze protein appears to be localized within the apoplast.

KW - apoplast

KW - cold-on-regulated gene

KW - ice recrystallization inhibition

KW - polygalacturonase inhibitor protein

KW - thermal hysteresis

KW - THERMAL HYSTERESIS PROTEIN

KW - N-LINKED OLIGOSACCHARIDES

KW - ICE RECRYSTALLIZATION

KW - WINTER RYE

KW - PLANT

KW - SEQUENCE

M3 - Article

SN - 0264-6021

VL - 340

SP - 385

EP - 391

JO - Biochemical journal

JF - Biochemical journal

ER -