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Divalent metal ion in the active site of purple acid phosphatase modulates substrate binding: Kinetic and thermodynamic properties
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Jul 1, 2024
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Abstract
The purple acid phosphatase was purified from 5.9-fold to apparent homogeneity from Anagelis arvensis seeds using SP-Sephadex C-50 and Sephadex G-100 chromatography. The results of residual activity tests conducted using different temperature ranges (50-70 °C) were calculated as the activation energy (E
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