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Substrate Specificity of Fucosyltransferase Purified from Human Parotid Saliva
H. Tamagawa
Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan
K. Iwakura
Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan
A. Amano
Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan
S. Shizukuishi
Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan
A. Tsunemitsu
Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan
The purified fucosyltransferase from human parotid saliva was shown to transfer fucose from GDP-fucose onto the oligosaccharide chains containing the Galβl 3GlcNAc or Gal β 1 4GlcNAc/Glc sequences. Competition studies between asialotransferrin and either lacto-N-fucopentaose 1 or 2'-fucosyllactose provided evidence that both the substrates competed for a common enzyme active site. These results suggest that the fucosyltransferase activities for the three acceptors may be catalyzed by the same enzyme.
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Journal of Dental Research, Vol. 66, No. 3,
756-760 (1987)
DOI: 10.1177/00220345870660031001

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