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Journal of Dental Research
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Purification and Some Properties of Fucosyltransferase in Human Parotid Saliva

H. Tamagawa

Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan

E. Inoshita

Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan

T. Takeshita

Department of Preventive Dentistry, Osaka University Faculty of Dentistry, 1-8, Yamadaoka, Suita, Osaka 565, Japan

M. Takagaki

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

Fucosyltransferase was purified from human parotid saliva by affinity chromatography on GDP-hexanolamine Sepharose, followed by chromatofocusing on PBE 94 exchanger gel. The purified enzyme had the N-acetylglucosaminide {alpha}1->4, the N-acetylglucosaminide {alpha}1->3, and the glucoside {alpha}1->3 fucosyltransferase activities. The molecular weight of the purified enzyme was estimated to be approximately 20,000. These enzyme activities showed identical pH and divalent metal ion dependencies and identical rates of inactivation upon being heated. The paper chromatographic analysis of the fucosylated products by the purified enzyme and the susceptibility of these products to linkage-specific fucosidase digestion indicated that the transferase formed the Fuc {alpha}1->4GlcNAc, Fuc {alpha}1->3GlcNAc, and Fuc {alpha}1->3Glc linkages.

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Journal of Dental Research, Vol. 66, No. 1, 72-77 (1987)
DOI: 10.1177/00220345870660011601
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[Abstract] [Full Text] [PDF]

This Article
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