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

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Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota). / Smallwood, M ; Worrall, D ; Byass, L et al.

In: Biochemical Journal, Vol. 340, No. 2, 01.06.1999, p. 385-391.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Smallwood, M, Worrall, D, Byass, L, Elias, L, Ashford, D, Doucet, CJ, Holt, C, Telford, J, Lillford, P & Bowles, DJ 1999, 'Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota)', Biochemical Journal, vol. 340, no. 2, pp. 385-391. <http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220261/>

APA

Smallwood, M., Worrall, D., Byass, L., Elias, L., Ashford, D., Doucet, C. J., Holt, C., Telford, J., Lillford, P., & Bowles, D. J. (1999). Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota). Biochemical Journal, 340(2), 385-391. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220261/

Vancouver

Smallwood M, Worrall D, Byass L, Elias L, Ashford D, Doucet CJ et al. Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota). Biochemical Journal. 1999 Jun 1;340(2):385-391.

Author

Smallwood, M ; Worrall, D ; Byass, L et al. / Isolation and characterization of a novel antifreeze protein from carrot (Daucus carota). In: Biochemical Journal. 1999 ; Vol. 340, No. 2. pp. 385-391.

Bibtex

@article{31bad0411c54432c97d6459fe0ecdcab,
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.",
number = "2",

}

RIS

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 - Journal article

VL - 340

SP - 385

EP - 391

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - 2

ER -