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- W2017072413 abstract "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 [ 35 S]‐cysteine, and the amino acid analysis showed a 4% cysteine content. In the native state dsp28 is a dimer with a single subunit M r 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." @default.
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- W2017072413 date "1991-01-01" @default.
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- W2017072413 title "Dsp28: A desiccation stress protein inTenebrio molitor hemolymph" @default.
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- W2017072413 doi "https://doi.org/10.1002/arch.940170210" @default.
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