Penguin egg-white and polar fish blood-serum proteins.
The development of, and findings in, a long-term research program on penguin proteins and polar fish blood proteins are described. Two of the egg-white proteins from the Adelie penguin (Pygoscelis adeliae) have unique properties: a glycoprotein named penalbumin that is a major constituent with some characteristics similar to ovalbumin, and an ovomucoid with strong inhibitory capacity for subtilisin as well as for bovine trypsin and alpha-chymotrypsin. The antifreeze glycoproteins from Antarctic fish (Trematomus borchgrevinki and Dissostichus mawsoni) and an Arctic fish (Boreogadus saida) appear to function noncolligatively by lowering the freezing temperature without affecting the melting point. Current evidence indicates that the antifreeze glycoprotein functions at the ice-solution interface, either on the ice surface or in a transition layer between the solution and the ice.
D000818:Animals; D000864:Antarctic Regions; D021301:Antifreeze Proteins; D001110:Arctic Regions; D005075:Biological Evolution; D001717:Birds / Q000502:physiology*; D001798:Blood Proteins / Q000502:physiology*; D003081:Cold Climate; D004527:Egg Proteins / Q000502:physiology*; D004529:Egg White; D005260:Female; D005399:Fishes / Q000097:blood*; D005615:Freezing; D006023:Glycoproteins / Q000502:physiology*; D010059:Ovomucin / Q000502:physiology; D013045:Species Specificity
D021301:Antifreeze Proteins; D001798:Blood Proteins; D004527:Egg Proteins; D006023:Glycoproteins; C035619:penalbumin protein, Pygoscelis adeliae; D010059:Ovomucin