Co2+ is able to substitute for Mn2+ in some exogenous and endogenous galactosyltransferase reactions.
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.
D000818:Animals; D002417:Cattle; D003035:Cobalt / Q000378:metabolism*; D005690:Galactose / Q000378:metabolism; D005700:Galactosyltransferases / Q000097:blood / Q000378:metabolism*; D006801:Humans; D008345:Manganese / Q000378:metabolism*; D008892:Milk / Q000201:enzymology; D051381:Rats; D014407:Tumor Cells, Cultured
D003035:Cobalt; D008345:Manganese; D005700:Galactosyltransferases; D005690:Galactose