## Abstract 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 coldβacclimated larvae of the beetle, __Tenebrio molitor__. Both proteins have unusual amino acid
Composition of a protein antifreeze from larvae of the beetle, Tenebrio molitor
β Scribed by Patterson, Jean L. ;Duman, John G.
- Publisher
- John Wiley and Sons
- Year
- 1979
- Tongue
- English
- Weight
- 305 KB
- Volume
- 210
- Category
- Article
- ISSN
- 0022-104X
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β¦ Synopsis
Abstract
A thermal hysteresis producing antifreeze protein was isolated from larvae of the beetle, Tenebrio molitor. This is the first thermal hysteresis protein purified from an insect. The specific activity of the Tenebrio antifreeze is somewhat greater than that of the fishes. The composition of the Tenebrio protein is quite different from those of the fish protein antifreezes. The most obvious difference is the lack of a large alanine component in the Tenebrio antifreeze. The significance of the differences are discussed.
π SIMILAR VOLUMES
Sex pheromone activity from female medwonn beetles (Tenebrio molitor) may be extracted and quantified by fractional population response of virgin adult males, which attempt copulation with any pheromone-treated object. Extracts of mature males can be shown to elicit identical behavioral activity, al