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Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne

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Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne. / Kumble, Krishnanand D.; Demmer, Jerome; Fish, Steven Anthony et al.
In: Cryobiology, Vol. 57, No. 3, 12.2008, p. 263-268.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Kumble, KD, Demmer, J, Fish, SA, Hall, C, Corrales, S, DeAth, A, Elton, C, Prestidge, R, Luxmanan, S, Marshall, CJ & Wharton, DA 2008, 'Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne', Cryobiology, vol. 57, no. 3, pp. 263-268. https://doi.org/10.1016/j.cryobiol.2008.09.005

APA

Kumble, K. D., Demmer, J., Fish, S. A., Hall, C., Corrales, S., DeAth, A., Elton, C., Prestidge, R., Luxmanan, S., Marshall, C. J., & Wharton, D. A. (2008). Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne. Cryobiology, 57(3), 263-268. https://doi.org/10.1016/j.cryobiol.2008.09.005

Vancouver

Kumble KD, Demmer J, Fish SA, Hall C, Corrales S, DeAth A et al. Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne. Cryobiology. 2008 Dec;57(3):263-268. Epub 2008 Sept 19. doi: 10.1016/j.cryobiol.2008.09.005

Author

Kumble, Krishnanand D. ; Demmer, Jerome ; Fish, Steven Anthony et al. / Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne. In: Cryobiology. 2008 ; Vol. 57, No. 3. pp. 263-268.

Bibtex

@article{9744fa1c5809497a9b529c72134ce9c0,
title = "Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne",
abstract = "Five genes coding for ice-active proteins were identified from an expressed sequence tag database of Lolium perenne cDNA libraries. Each of the five genes were characterized by the presence of an N-terminal signal peptide, a region enriched in hydrophilic amino acids and a leucine-rich region in four of the five genes that is homologous with the receptor domain of receptor-like protein kinases of plants. The C-terminal region of all five genes contains sequence homologous with Lolium and Triticum ice-active proteins. Of the four ice-active proteins (IAP1, IAP2, IAP3 and IAP5) cloned, three could be expressed in Escherichia coli and recovered in a functional form in order to study their ice activity. All three ice-active proteins had recrystallization inhibition activity but showed no detectable antifreeze or ice nucleation activity at the concentration tested. IAP2 and LAP5 formed distinct hexagonal-shaped crystals in the nanolitre osmometer as compared to the weakly hexagonal crystals produced by IAP3.",
keywords = "Antifreeze protein, Recrystallization inhibition, Thermal hysteresis, Ice nucleation, Ryegrass, Lolium perenne, Ice-active protein",
author = "Kumble, {Krishnanand D.} and Jerome Demmer and Fish, {Steven Anthony} and Claire Hall and Sofia Corrales and Angela DeAth and Clare Elton and Ross Prestidge and Selvanesan Luxmanan and Marshall, {Craig J.} and Wharton, {David A.}",
year = "2008",
month = dec,
doi = "10.1016/j.cryobiol.2008.09.005",
language = "English",
volume = "57",
pages = "263--268",
journal = "Cryobiology",
number = "3",

}

RIS

TY - JOUR

T1 - Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne

AU - Kumble, Krishnanand D.

AU - Demmer, Jerome

AU - Fish, Steven Anthony

AU - Hall, Claire

AU - Corrales, Sofia

AU - DeAth, Angela

AU - Elton, Clare

AU - Prestidge, Ross

AU - Luxmanan, Selvanesan

AU - Marshall, Craig J.

AU - Wharton, David A.

PY - 2008/12

Y1 - 2008/12

N2 - Five genes coding for ice-active proteins were identified from an expressed sequence tag database of Lolium perenne cDNA libraries. Each of the five genes were characterized by the presence of an N-terminal signal peptide, a region enriched in hydrophilic amino acids and a leucine-rich region in four of the five genes that is homologous with the receptor domain of receptor-like protein kinases of plants. The C-terminal region of all five genes contains sequence homologous with Lolium and Triticum ice-active proteins. Of the four ice-active proteins (IAP1, IAP2, IAP3 and IAP5) cloned, three could be expressed in Escherichia coli and recovered in a functional form in order to study their ice activity. All three ice-active proteins had recrystallization inhibition activity but showed no detectable antifreeze or ice nucleation activity at the concentration tested. IAP2 and LAP5 formed distinct hexagonal-shaped crystals in the nanolitre osmometer as compared to the weakly hexagonal crystals produced by IAP3.

AB - Five genes coding for ice-active proteins were identified from an expressed sequence tag database of Lolium perenne cDNA libraries. Each of the five genes were characterized by the presence of an N-terminal signal peptide, a region enriched in hydrophilic amino acids and a leucine-rich region in four of the five genes that is homologous with the receptor domain of receptor-like protein kinases of plants. The C-terminal region of all five genes contains sequence homologous with Lolium and Triticum ice-active proteins. Of the four ice-active proteins (IAP1, IAP2, IAP3 and IAP5) cloned, three could be expressed in Escherichia coli and recovered in a functional form in order to study their ice activity. All three ice-active proteins had recrystallization inhibition activity but showed no detectable antifreeze or ice nucleation activity at the concentration tested. IAP2 and LAP5 formed distinct hexagonal-shaped crystals in the nanolitre osmometer as compared to the weakly hexagonal crystals produced by IAP3.

KW - Antifreeze protein

KW - Recrystallization inhibition

KW - Thermal hysteresis

KW - Ice nucleation

KW - Ryegrass

KW - Lolium perenne

KW - Ice-active protein

U2 - 10.1016/j.cryobiol.2008.09.005

DO - 10.1016/j.cryobiol.2008.09.005

M3 - Journal article

VL - 57

SP - 263

EP - 268

JO - Cryobiology

JF - Cryobiology

IS - 3

ER -