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Although the two fish orders have similar antifreeze proteins, cod species contain arginine in AFG, while Antarctic notothenioid do not. [38] The role of arginine as an enhancer has been investigated in Dendroides canadensis antifreeze protein (DAFP-1) by observing the effect of a chemical modification using 1-2 cyclohexanedione. [ 39 ]
A cryoprotectant is a substance used to protect biological tissue from freezing damage (i.e. that due to ice formation). Arctic and Antarctic insects, fish and amphibians create cryoprotectants (antifreeze compounds and antifreeze proteins) in their bodies to minimize freezing damage during cold winter periods.
Some non-Antarctic species either produce no or very little antifreeze, and antifreeze concentrations in some species are very low in young, larval fish. [3] They also possess aglomerular kidneys, an adaptation that aids the retention of these antifreeze proteins. [16]
The concentration of antifreeze glycoproteins can vary with differing environmental conditions, such as colder environments caused by location. Larger amounts of the proteins have been found in species with habitats in higher latitudes, due to the higher expression of the protein and longer degradation time compared to relatives in more ...
This species and other species in the Trematomus genus have two antifreeze proteins (AFPs): antifreeze glycoproteins (AFGPs) and antifreeze potentiating proteins (AFPPs). These AFPs absorb to internal ice crystals that would inhibit growth and lower the freezing point of these species' blood to below the freezing point of the surrounding ...
Like most other Antarctic notothenioids, the blackfin icefish produces antifreeze glycoproteins in their blood and other body fluids. [15] These proteins reduce the internal freezing temperature, preventing ice crystallization and thus allowing the fish to survive in water below 0 °C.
The evolution of the antifreeze protein in L. dearborni provides a prime example of neofunctionalization after gene duplication. In the case of the Antarctic zoarcid fish type III antifreeze protein gene (AFPIII; P12102 ) diverged from a paralogous copy of sialic acid synthase (SAS) gene. [ 9 ]
The evolution of the antifreeze protein in the Antarctic zoarcid fish Lycodichthys dearborni provides a prime example of neofunctionalization after gene duplication. In the case of the Antarctic zoarcid fish type III antifreeze protein gene (AFPIII; P12102 ) diverged from a paralogous copy of sialic acid synthase (SAS) gene. [ 13 ]