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- W2046807798 abstract "Aqualysin I has at least two Ca2+-binding sites that have different affinities for Ca2+. The binding of various metal ions to aqualysin I was studied using 23Na- and 139La-NMR spectrometry. Evidence is presented that Ca2+, La3+, and Na+ bind to the low-affinity Ca2+-binding site of aqualysin I, but Mg2+ does not. Our results confirm that binding of metals at the low-affinity Ca2+-binding site is essential for thermostabilization, since the addition of Mg2+ did not result in thermostabilization. La3+ was found to bind to both the low-affinity Ca2+-binding site and an additional metal ion-binding site that can also be involved in the thermostabilization of aqualysin I." @default.
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- W2046807798 date "2002-01-01" @default.
- W2046807798 modified "2023-10-02" @default.
- W2046807798 title "Sodium-23 and Lanthanum-139 Nuclear Magnetic Resonance Studies of Cation Binding to Aqualysin I, a Thermostable Serine Protease" @default.
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- W2046807798 doi "https://doi.org/10.1271/bbb.66.1281" @default.
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