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

Kumble, Krishnanand D. and Demmer, Jerome and Fish, Steven Anthony and Hall, Claire and Corrales, Sofia and DeAth, Angela and Elton, Clare and Prestidge, Ross and Luxmanan, Selvanesan and Marshall, Craig J. and Wharton, David A. (2008) Characterization of a family of ice-active proteins from the Ryegrass, Lolium perenne. Cryobiology, 57 (3). pp. 263-268.

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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.

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06 May 2016 14:08
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01 Feb 2022 04:56