Abstract
Addition of magnesium to apo-concanavalin A in the presence of calcium was shown by ultraviolet difference spectroscopy to generate a holoprotein spectroscopically identical to the MnCa-holoprotein. The MgCa- and MnCa-forms bound equally strongly to Sephadex G-75. In kinetic experiments, the binding of Mg 2+ was much slower than Mn 2+ binding; K d for Mg 2+ was estimated as 7.4 mM. The combined Mg 2+ and Mn 2+ contents of 10 lectins specific for D-galactose or N-acetyl-D-galactosamine were each close to one atom per subunit, suggesting occupancy of the Mn 2+ site by Mg 2+ is common in plant lectins.
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