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Purification and Some Properties of Neuraminidase Isolated from the Culture Medium of Oral Bacterium Streptococcus mitis ATCC 9811
H. Nonaka
Department of Preventive Dentistry, School of Dentistry, The University of Tokushima, Kuramotocho 3-chome, Tokushima City 770, Japan
Y. Ishikawa
Department of Preventive Dentistry, School of Dentistry, The University of Tokushima, Kuramotocho 3-chome, Tokushima City 770, Japan
M. Otsuka
Department of Preventive Dentistry, School of Dentistry, The University of Tokushima, Kuramotocho 3-chome, Tokushima City 770, Japan
K. Toda
Department of Preventive Dentistry, School of Dentistry, The University of Tokushima, Kuramotocho 3-chome, Tokushima City 770, Japan
M. Sato
Department of Preventive Dentistry, School of Dentistry, The University of Tokushima, Kuramotocho 3-chome, Tokushima City 770, Japan
R. Nakamura
Department of Preventive Dentistry, School of Dentistry, The University of Tokushima, Kuramotocho 3-chome, Tokushima City 770, Japan
Neuraminidase acting on the salivary bacterial agglutinating factor was isolated and purified from the culture medium of Streptococcus mitis ATCC 9811. The molecular weight and the isoelectric point of the enzyme were determined to be 42,000 and a pH of 4.6, respectively. The enzyme showed high activity against human glycoprotein substraes, especially the salivary bacterial agglutinating factor.
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Journal of Dental Research, Vol. 62, No. 7,
792-797 (1983)
DOI: 10.1177/00220345830620070301

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