Galactosyl-and fucosyltransferases in etiolated pea epicotyls: product identification and sub-cellular localisation

Abstract

Particulate membrane preparations from etiolated pea epicotyls were found to contain fucosyltransferases, which transferred fucose from GDP-fucose onto xyloglucan and N-linked glycoprotein, and galactosyltransferases, which transferred galactose from UDP-galactose onto galactan, xyloglucan, and N-linked glycoprotein. The products were characterised by specific enzyme degradation and by acid and alkaline hydrolysis. All the enzymes were found to be concentrated in the Golgi apparatus. The Golgi apparatus was further fractionated into membranes of low, medium and high-density. The glycoprotein fucosyltransferase activity was present in highest amounts in the medium-density Golgi membranes, while the majority of the xyloglucan fucosyltransferase was present in the low-density Golgi membranes. The majority of the galactan galactosyltransferase (galactan synthase) was found in the low-density membranes, while the glycoprotein galactosyltransferase was equally distributed in all three subfractions.