Purification and characterization of galactosyltransferase in human parotid saliva.
The galactosyltransferase has been purified from human parotid saliva by ammonium sulfate precipitation (25-70% saturation), followed by repeated affinity chromatography on Sepharose-alpha-lactalbumin. The molecular weight of the enzyme was estimated to be approximately 56,000. The enzyme catalyzes the transfer of galactose from UDP-galactose to the exposed N-acetylglucosamine residues derived from glycoproteins, forming a Gal beta (1-4)GlcNAc linkage.
D000328:Adult; D001665:Binding Sites; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D005700:Galactosyltransferases / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D010306:Parotid Gland; D012463:Saliva / Q000201:enzymology*; D012471:Salivary Proteins and Peptides / Q000032:analysis
D012471:Salivary Proteins and Peptides; D005700:Galactosyltransferases