Existence of a Tungsten-Binding Protein in Acidithiobacillus ferrooxidans AP19-3(ENVIRONMENTAL BIOTECHNOLOGY)

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A tungsten-binding protein was purified from a plasma membrane preparation of the iron-oxi-dizing bacterium, Acidithiobacillus ferrooxidans AP19-3 in an electrophoretically homogenous state. The protein was composed of two subunits with apparent molecular masses of 12 and 20.7 kDa. The molecular mass of the native protein was estimated to be 26.4 kDa in the presence of 1.5% 1-o-octyl-D-glucopyranoside (OGL), indicating that the native tungsten-binding protein is a heterodimeric protein. The amounts of tungsten bound to 1 mg of plasma membranes of A. ferrooxidans AP19-3 and the purified tungsten-binding protein at pH3.0 were 191 and 1506 μg, respectively. In contrast, the amounts of tungsten bound to 1 mg of albumin, aldolase, catalase, chymotrypsinogen A, ferritin, and ferredoxin at pH3.0 were 13.1, 18.6, 12.8, 16.6, 11.4, and 6.1 μg, respectively. Incubation of the tungsten-binding protein for 1 h with 10 mM Na_2WO_4 plus 10 mM metal ion, such as NaVO_3, Na_2MoO_4, CuSO_4, NiSO_4, MnSO_4, CoSO_4, or CdCl_2, did not markedly affect the amount of tungsten bound to the tungsten-binding protein, suggesting that the protein specifically binds tungsten.
社団法人日本生物工学会の論文
2004-06-25