Abstract
The ability of Co2+ to substitute for Mn2+ in exogenous and endogenous galactosyltransferase reactions was tested. Exogenous transfer was measured towards different high and low molecular weight galactose acceptors using galactosyltransferase from the following sources: crude serum, the serum enzyme partially purified by affinity chromatography and a pure enzyme preparation from milk. Endogenous transfer was estimated in preparations from human urinary bladder tumor cells and from rat liver microsomal fractions. The results show that Co2+ is able to substitute for Mn2+ in some exogenous and endogenous galactosyltransferase reactions. This ability seems to depend on the molecular structure of the galactose acceptor as well as on the nature of the enzyme.
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