期刊
CRYOBIOLOGY
卷 57, 期 3, 页码 263-268出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.cryobiol.2008.09.005
关键词
Antifreeze protein; Recrystallization inhibition; Thermal hysteresis; Ice nucleation; Ryegrass; Lolium perenne; Ice-active protein
资金
- Genesis Research and Development Corporation Limited
- PGG Wrightson Seeds Limited
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. (C) 2008 Elsevier Inc. All rights reserved.
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