{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,4]],"date-time":"2026-05-04T04:27:28Z","timestamp":1777868848469,"version":"3.51.4"},"reference-count":0,"publisher":"S. Karger AG","license":[{"start":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T00:00:00Z","timestamp":1502409600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"},{"start":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T00:00:00Z","timestamp":1502409600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/karger.com\/pages\/terms-and-conditions"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Enzyme"],"abstract":"<jats:p>Using 4-methylumbelliferyl-N-acetylneuraminic acid (4MU-NeuAc) as substrate,\nwe measured sialidase activity in the salivary glands and other organs of the rat. The\npH optima of salivary gland sialidase were between 4.0 and 4.5, which were similar to those\nof the enzyme in the brain, liver and kidney. Among the salivary glands, the submandibular\none showed the highest sialidase activity followed by the parotid and the sublingual glands.\nHowever, sialidase activity in these glands was lower when compared with the activity in the\nbrain, liver and kidney. From the subcellular distribution study, salivary gland sialidase was\nfound to be mainly localized in the lysosomes. The pH optima of the lysosomal sialidase of\nthe salivary glands were between 4.0 and 4.5; and K(m) values for 4MU-NeuAc approximately\n0.09 mmol\/1. In the submandibular and parotid glands, a soluble sialidase with a different\npH optimum (5.5) and K(m) value (0.25 mmol\/1) was also detected.<\/jats:p>","DOI":"10.1159\/000469079","type":"journal-article","created":{"date-parts":[[2017,8,11]],"date-time":"2017-08-11T17:21:39Z","timestamp":1502472099000},"page":"200-208","source":"Crossref","is-referenced-by-count":3,"title":["Characteristics of Sialidase in the Rat Salivary Glands"],"prefix":"10.1159","author":[{"given":"Akinao","family":"Sato","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masahiko","family":"Hiramatsu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Masanori","family":"Kashimata","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Makoto","family":"Murayama","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naoyuki","family":"Minami","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Naomi","family":"Minami","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"127","published-online":{"date-parts":[[2017,8,11]]},"container-title":["Enzyme"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/karger.com\/article-pdf\/doi\/10.1159\/000469079","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,4,30]],"date-time":"2026-04-30T12:46:38Z","timestamp":1777553198000},"score":1,"resource":{"primary":{"URL":"https:\/\/karger.com\/article\/doi\/10.1159\/000469079"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,8,11]]},"references-count":0,"URL":"https:\/\/doi.org\/10.1159\/000469079","archive":["Portico"],"relation":{},"ISSN":["0013-9432","2504-2564"],"issn-type":[{"value":"0013-9432","type":"print"},{"value":"2504-2564","type":"electronic"}],"subject":[],"published":{"date-parts":[[2017,8,11]]}}}