Dsp28: A desiccation stress protein in Tenebrio molitor hemolymph

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Abstract
A novel hemolymph protein from Tenebrio molitor associated with desiccation stress has been purified and characterized. The protein contains cysteine; it was labeled in vivo using [35S]‐cysteine, and the amino acid analysis showed a 4% cysteine content. In the native state dsp28 is a dimer with a single subunit Mr of 28,000. The synthesis of dsp28 and its concentration in larval hemolymph increase dramatically after desiccation. Dsp28 is a major component of total larval hemolymph protein representing 5% of total protein in control insects and up to 17% in desiccated larvae. The hemolymph of cold‐acclimated larvae also contains elevated levels of dsp28.