Abstract
Research on penguin proteins and polar fish blood proteins is described. Two of the egg-white proteins from the Adelie penguin (P. 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. The antifreeze glycoprotein evidently functions at the ice-solution interface, either on the ice surface or in a transition layer between the solution and the ice.