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• W2009596324 abstract "The interaction of Li + with myo ‐inositol monophosphatase was studied by 7 Li‐NMR spectroscopy. Li + binding to the enzyme induces a downfield shift and broadening of the 7 Li‐NMR signal. Changes of the chemical shift were used to follow the titration of the enzyme with lithium and to determine a dissociation constant, K d = (1.0 ± 0.1) mM. Only one major binding site/enzyme subunit was inferred. The complex forms independently of the presence of inorganic phosphate. Metals from the group IIa of the periodic table compete with Li + binding with the affinity increasing in the order Mg 2+ < Ca 2+ Be 2+ . In contrast to lithium, their binding is enhanced by phosphate." @default.
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• W2009596324 date "1996-08-01" @default.
• W2009596324 modified "2023-10-18" @default.
• W2009596324 title "⁷Li Nuclear-Magnetic-Resonance Study of Lithium Binding to<i>Myo</i>-Inositol Monophosphatase" @default.
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• W2009596324 doi "https://doi.org/10.1111/j.1432-1033.1996.0288h.x" @default.
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