TY - JOUR
T1 - Re-evaluation of the binding of ATP to metallothionein
AU - Zangger, Klaus
AU - Öz, Gülin
AU - Armitage, Ian M.
PY - 2000/3/17
Y1 - 2000/3/17
N2 - In a recent paper Jiang et al. (Jiang, L. J., Maret, W. and 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 μM 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.
AB - In a recent paper Jiang et al. (Jiang, L. J., Maret, W. and 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 μM 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.
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U2 - 10.1074/jbc.275.11.7534
DO - 10.1074/jbc.275.11.7534
M3 - Article
C2 - 10713058
AN - SCOPUS:0040951508
SN - 0021-9258
VL - 275
SP - 7534
EP - 7538
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 11
ER -