Re-evaluation of the binding of ATP to metallothionein.
In a recent paper Jiang et al. (Jiang, L. J., Maret, W. & Vallee, B. L. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 9146-9149) reported that metallothionein interacts with adenosine triphosphate (ATP) to form a 1:1 complex with a dissociation constant of K(d) = 176 +/- 33 microM at pH 7.4. In an effort to characterize further this interaction using nuclear magnetic resonance spectroscopy, titration calorimetry, gel-filtration chromatography, affinity chromatography, and ultrafiltration, we were unable to find any evidence for the binding of ATP to metallothionein.
Zangger
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Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA.
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Armitage
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D000255:Adenosine Triphosphate / Q000378:metabolism*; D002151:Calorimetry; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D008668:Metallothionein / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular
D000255:Adenosine Triphosphate; D008668:Metallothionein