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Purification and Some Properties of a-L-Fucosidase Isolated from Streptococcus sanguisDepartment of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka, 530 Japan, Research Laboratory of Oral Biology, Sunstar, Inc., Takatsuki, Osaka, 569 Japan
Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka, 530 Japan, Research Laboratory of Oral Biology, Sunstar, Inc., Takatsuki, Osaka, 569 Japan
Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka, 530 Japan, Research Laboratory of Oral Biology, Sunstar, Inc., Takatsuki, Osaka, 569 Japan
Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka, 530 Japan, Research Laboratory of Oral Biology, Sunstar, Inc., Takatsuki, Osaka, 569 Japan
Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka, 530 Japan, Research Laboratory of Oral Biology, Sunstar, Inc., Takatsuki, Osaka, 569 Japan
Department of Preventive Dentistry, Osaka University Dental School, Kitaku, Osaka, 530 Japan, Research Laboratory of Oral Biology, Sunstar, Inc., Takatsuki, Osaka, 569 Japan
Journal of Dental Research, Vol. 57, No. 11,
1028-1035 (1978) This article has been cited by other articles:
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-L-Fucosidase acting on naturally occurring substrates was highly purified from the growth culture of Streptococcus sanguis ATCC 10557. The molecular weight of the enzyme was approximately 120,000 and the optimal pH was at 5.5. The purified enzyme showed specificity toward the linkage of
2) fucosides in oligosaccharides and glycoproteins. The enzyme released L-fucose from glycoprotein in human parotid saliva. 
