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. 1983 Jul;62(7):792-7.
doi: 10.1177/00220345830620070301.

Purification and some properties of neuraminidase isolated from the culture medium of oral bacterium Streptococcus mitis ATCC 9811

H Nonaka, Y Ishikawa, M Otsuka, K Toda, M Sato, R Nakamura

Purification and some properties of neuraminidase isolated from the culture medium of oral bacterium Streptococcus mitis ATCC 9811

H Nonaka et al. J Dent Res. 1983 Jul.

Abstract

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 substrates, especially the salivary bacterial agglutinating factor.

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