Enzyme

Original Paper

Characteristics of Sialidase in the Rat Salivary Glands

Sato A. · Hiramatsu M. · Kashimata M. · Murayama M. · Minami N. · Minami N.

Author affiliations

Department of Dental Pharmacology, Josai Dental University, Saitama, Japan

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Enzyme 1989;41:200–208

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Article / Publication Details

Published online: August 11, 2017
Issue release date: 1989

Number of Print Pages: 9
Number of Figures: 0
Number of Tables: 0

ISSN: 0013-9432 (Print)
eISSN: 2504-2564 (Online)

For additional information: https://www.karger.com/EZD

Abstract

Using 4-methylumbelliferyl-N-acetylneuraminic acid (4MU-NeuAc) as substrate, we measured sialidase activity in the salivary glands and other organs of the rat. The pH optima of salivary gland sialidase were between 4.0 and 4.5, which were similar to those of the enzyme in the brain, liver and kidney. Among the salivary glands, the submandibular one showed the highest sialidase activity followed by the parotid and the sublingual glands. However, sialidase activity in these glands was lower when compared with the activity in the brain, liver and kidney. From the subcellular distribution study, salivary gland sialidase was found to be mainly localized in the lysosomes. The pH optima of the lysosomal sialidase of the salivary glands were between 4.0 and 4.5; and K(m) values for 4MU-NeuAc approximately 0.09 mmol/1. In the submandibular and parotid glands, a soluble sialidase with a different pH optimum (5.5) and K(m) value (0.25 mmol/1) was also detected.




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Article / Publication Details

Published online: August 11, 2017
Issue release date: 1989

Number of Print Pages: 9
Number of Figures: 0
Number of Tables: 0

ISSN: 0013-9432 (Print)
eISSN: 2504-2564 (Online)

For additional information: https://www.karger.com/EZD


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