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

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