Abstract
The article reviews the studies of the authors and other investigators on blood proteins and muscle and brain enzymes from Antarctic fishes adapted to the −1.85 °C temperature of the ice-salt water of McMurdo Sound, Antarctica. The bloods had two major characteristics related to the cold-adaptation: a rapid rate of clotting of the blood at 0 °C and a very specialized type of glycoprotein (antifreeze protein) responsible for the prevention of freezing of the blood. This antifreeze protein has the repeating structure of a glycotripeptide consisting of units of alanine, alanine, threonine with each threonine glycosidically linked to a disaccharide of galactosyl-N-acetyl galactosamine. Six enzymes studied were muscle fructose-1,6-diphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, glycogen phosphorylase, and lactic dehydrogenase, heart mitochondrial cytochrome system, and brain tissue acetylcholinesterase. Adaptations for efficient catalysis at low temperatures included a low activation energy (for catalysis) and a resistance to inactivation at low temperature, but there was no general property characteristic of low temperature adaptation.
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