Identity of GA1, GM1a and GD1b synthase in Golgi vesicles from rat liver.
Synthesis of ganglioside GD1b from ganglioside GD2 was demonstrated using Golgi membranes isolated from rat liver. Competition experiments using gangliosides GA2, GM2 and GD2 as substrates, and as mutual inhibitors for ganglioside galactosyltransferase activity in preparations of Golgi vesicles derived from rat liver, suggested that galactosyl transfer to these three compounds, leading to gangliosides GA1, GM1a and GD1b respectively, is catalyzed by one enzyme. These results strengthen the hypothesis that the main site for the regulation of ganglioside biosynthesis occurs within the reaction sequence LacCer----GA3----GD3----GT3.
Iber
H
H
Institut für Organische Chemie and Biochemie, Universität Bonn, FRG.
Kaufmann
R
R
Pohlentz
G
G
Schwarzmann
G
G
Sandhoff
K
K
D000818:Animals; D001665:Binding Sites; D005700:Galactosyltransferases / Q000378:metabolism*; D005732:Gangliosides / Q000096:biosynthesis*; D006056:Golgi Apparatus / Q000201:enzymology*; D008099:Liver / Q000201:enzymology* / Q000378:metabolism; D008433:Mathematics; D051381:Rats; D012799:Sialyltransferases / Q000378:metabolism*
D005732:Gangliosides; D005700:Galactosyltransferases; D012799:Sialyltransferases