Two antifreeze proteins with thermal hysteresis activity (they depress the freezing point of aqueous solutions by a noncolligative mechanism well below the melting point) were purified from cold‐acclimated larvae of the beetle, Tenebrio molitor. Both proteins have unusual amino acid compositions consisting of high levels of cysteine (15.4 and 28.0 mol%).
|Original language||English (US)|
|Number of pages||4|
|Journal||Journal of Experimental Zoology|
|State||Published - 1982|
ASJC Scopus subject areas
- Animal Science and Zoology