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Journal of Dental Research, Vol 59, 1374-1381, Copyright © 1980 by International & American Associations for Dental Research Online Journals

ARTICLES

Purification and characterization of galactosyltransferase in human parotid saliva

R. Nakamura, T. Taniguchi, H. Nonaka, S. Shizukuishi and A. Tsunemitsu

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.




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