Sialyltransferases in young rat brain.
1. There are more glycolipid acceptor sites for NeuNAc than for glycoproteins in 11--15 day old rat cerebra. 2. The glycolipid acceptors appear to be almost exclusively Cer-Glc-Gal and GM1 ganglioside and each is a substrate for a different sialyltransferase. 3. The sialyltransferase(s) that acted on glycoprotein could be differentiated from the ones that acted on the glycolipids. 4. The apparent Km for CMP-NeuNAc was the same for all four of the sialyltransferase reactions studied. 5. Electron microscopic examination and marker enzyme studies on continuous sucrose gradient fractions found that most of the sialyltransferase activities appeared to be localized in smooth microsomal membrane and the Golgi complex derivatives and not associated with the synaptosomes.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid; D006017:Glycolipids / Q000096:biosynthesis; D006023:Glycoproteins / Q000096:biosynthesis; D006358:Hot Temperature; D007700:Kinetics; D051381:Rats; D012799:Sialyltransferases / Q000378:metabolism*; D013347:Subcellular Fractions / Q000201:enzymology; D014166:Transferases / Q000378:metabolism*; D000509:alpha-Fetoproteins
D006017:Glycolipids; D006023:Glycoproteins; D000509:alpha-Fetoproteins; D003569:Cytidine Monophosphate N-Acetylneuraminic Acid; D014166:Transferases; D012799:Sialyltransferases