Purification and Some Properties of Metal-binding Proteins in Housefly Larvae (Musca domestica)

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Cadmium and zinc-binding proteins similar to metallothionein have been isolated from housefly larvae (Musca domestica) exposed to cadmium chloride. Amino acid composition analysis found a high half-cystine content and an apparent minimum molecular weight of 5225. Metal-binding proteins of Musca domestica contained 3.9 g-atoms and 4.5 g-atoms of heavy metals per mole, respectively, and showed the spectral characteristic of cadmium-thionein, i. e., a broad shoulder at 250 nm and low residual absorption at 280 nm. The simple and specific replacement of cadmium and zinc bound to the protein with a cupric ion indicates that proteins have mercaptide bonding with a high affinity for copper. The molecular weight of the proteins modified with Ellman's reagent was 5300±250 when measured by gel filtration in the presence of 6 M guanidine hydrochloride.
社団法人日本農芸化学会の論文
1993-11-23