Abstract
Antifreeze proteins, produced by many cold water marine teleost fish and terrestrial arthropods (insects, spiders, etc.), inhibit ice crystal growth by a non-colligative mechanism, probably by adsorbing onto the surface of potential seed ice crystals and thereby blocking growth at preferred growth sites. In this study it is demonstrated that the activity of two insect antifreeze proteins is greatly increased by the addition of specific rabbit polyclonal antibodies to the antifreezes. A model is presented which suggests that the enhancement occurs because the antifreeze-antibody complex, being much larger than the antifreeze protein alone (a minimal 7–8-fold increase in size), blocks a larger area of the ice crystal surface and extends further above the surface, thus requiring the temperature to be further lowered before crystal growth proceeds. This idea is further supported by the finding that addition of goat anti-rabbit IgG to the antifreeze protein + anti-antifreeze protein antibody complexes further enhanced activity.
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More From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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