UDP-galactose:lactosylceramide alpha-galactosyltransferase activity in human placenta.
The activity of UDP-Gal:LacCer galactosyltransferase in human placenta was studied by using crude homogenate and Triton CF-54 extract as the source of enzyme. Transfer of galactose to lactosylceramide was optimal in the presence of 0.1% Triton CF-54 and Mn2+ at pH 6.3, and the reaction product was susceptible to alpha-galactosidase.
Lampio
A
A
Department of Biochemistry, University of Helsinki, Finland.
Airaksinen
A
A
Maaheimo
H
H
D002240:Carbohydrate Sequence; D002855:Chromatography, Thin Layer; D003902:Detergents; D004795:Enzyme Stability; D005700:Galactosyltransferases / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010920:Placenta / Q000201:enzymology*; D012995:Solubility
D003902:Detergents; D005700:Galactosyltransferases; C045097:UDP-galactose-lactosylceramide alpha 1-4-galactosyltransferase