Abstract
Double reciprocal plots for galactosyl transferase with UDP-galactose varying at several fixed Mn 2+ concentrations are a series of straight lines. Different laboratories disagree as to whether the intercepts on the 1 v axis are independent of Mn 2+ or not. PbCl 2 added in a fixed proportion is shown theoretically to be incapable of introducing such a dependence on total metal ion concentration. A mechanism derived from extensive kinetic studies is presented, with alternative pathways for free UDP-galactose and the Mn 2+ complex as substrates, following obligatory Mn 2+ addition, and the conflicting results from different laboratories are explained on the basis of a different flux through the alternative pathways under different conditions.
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