We purified antifreeze proteins from winter-active snow fleas, Hypogastrura harveyi. These 6.5- and 15.7-kilodalton thermolabile proteins are glycine-rich (45% of the residues), and the short isoform is composed of the tripeptide repeat Gly-X-X. This makes them very different from other antifreeze proteins, including two from insects, suggesting independent adaptation to freezing environments.
No takes yet. Share an insight, caveat, or question.
Graham et al. (2005) studied this question.