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Journal of Dental Research
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Purification and Characterization of Galactosyltransferase in Human Parotid Saliva

Ryo Nakamura

Department of Preventive Dentistry, Tokushima University School of Dentistry, Kuramotocho, Tokushima City 770, Japan

Tateshi Taniguchi

Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka 530, Japan

Hideki Nonaka

Department of Preventive Dentistry, Tokushima University School of Dentistry, Kuramotocho, Tokushima City 770, Japan

Satoshi Shizukuishi

Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka 530, Japan

Akira Tsunemitsu

Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka 530, Japan

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 Galβ(1-4)GlcNAc linkage.

Journal of Dental Research, Vol. 59, No. 8, 1374-1381 (1980)
DOI: 10.1177/00220345800590080301
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