Previous studies have established that the capacity of the glycopeptide antifreezes to depress the freezing temperature of aqueous solutions is positively correlated with molecular weight. The present study was carried out to determine whether a similar correlation existed within the antifreeze peptides. Two approaches were used. Initially, the antifreeze activity (thermal hysteresis) curves of antifreeze peptides from winter flounder, Pseudopleuronectes americanus (molecular weight, 3300), shorthorn sculpin, Myoxocephalus scorpius (molecular weight, 4000), ocean pout, Macrozoarces americanus (molecular weight, 6000), and sea raven, Hemitripterus americanus (molecular weight, 9700), were compared. In the second approach, a more specific comparison was made of two different sized antifreeze peptide components (molecular weights, 2900 and 4000) from the shorthorn sculpin. In both approaches, antifreeze peptide activity was positively correlated with molecular weight and the curve illustrating this relationship suggests that any reduction in molecular weight below 3300 will result in a disproportionate decline in activity. The relatively small antifreeze peptides from the winter flounder and shorthorn sculpin had greater activity than did glycopeptide antifreezes of similar size. However, glycopeptide antifreezes with a molecular weight of 10 000 or more had activities that exceeded that of any known antifreeze peptide. Increases in molecular weight of antifreeze peptides above 4000 resulted in a decline in antifreeze activity per milligram protein. Therefore, in terms of ability to depress the freezing temperature, there appears to be no advantage in evolving large antifreeze peptide molecules.
N-methyl-D-aspartate receptors mediate chemoreflexes in the shorthorn sculpin Myoxocephalus scorpius
