Abstract
Antifreeze proteins (AFPs) are found in a wide range of species including fishes, plants, etc. They have very characteristic feature that inhibit the growth and recrystallization of ice that forms in intercellular spaces. Two expressed sequence tags (ESTs) were previously identified from salt stress cDNA library in Fragilariopsis cylindrus to have similarities with snow mold AFP. Using bioinformatics tools, we analysed these two AFP-ESTs. Accordingly, by using specially designed primers, the open reading frames (ORFs) subcloned into bacterial and plant expression vectors. The predicted gene product, AfpA, had a molecular mass of 27 kDa. Expression of afpA in Escherichia coli yielded an intracellular 27-kDa protein modified with His-tag. According to bioinformatics data, a comparison between AFP-A and carrot AFP has been carried out.
Highlights
Antifreeze proteins (AFPs) are family of proteins capable of protecting organisms from freezing or sub-freezing damage
FCylESTA46A10.s1 was rich in Ala and Gly amino acid, while carrot AFP was rich in Leu (Table 2)
FCylESTA46A10.s1 was rich in Met when compared with carrot AFP
Summary
Antifreeze proteins (AFPs) are family of proteins capable of protecting organisms from freezing or sub-freezing damage. TH activity of plant AFPs is less than that of fish AFPs and significantly less than that of insect. AFPs. On the other hand, plant AFPs has strong ice recrystallization inhibition (RI) activity (Sidebottom et al, 2000). Ice recrystallization is the growth of large ice crystals in the expense of the smaller ones. Inhibition of this process has great effect on decreasing cellular damage (Knight et al, 1984)
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