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We investigated the biochemical characteristics of these ectoenzymes in cells cultured from submandibular salivary glands of rats. The<jats:italic>V<\/jats:italic><jats:sub>max<\/jats:sub>for the hydrolysis of ATP, ADP and AMP were 2275 \u00b1 153 (mean \u00b1 SEM,<jats:italic>n<\/jats:italic>= 4), 941 \u00b1 96 (mean \u00b1 SEM,<jats:italic>n<\/jats:italic>= 5) and 175 \u00b1 5 (mean \u00b1 SEM,<jats:italic>n<\/jats:italic>= 5) nmol Pi liberated per min per mg of protein, respectively. The<jats:italic>K<\/jats:italic><jats:sub>m<\/jats:sub>values for ATP, ADP and AMP were 224 \u00b1 8 \u03bcM (mean \u00b1 SEM,<jats:italic>n<\/jats:italic>= 4), 163 \u00b1 15 \u03bcM (mean \u00b1 SEM,<jats:italic>n<\/jats:italic>= 5) and 117 \u00b1 5 \u03bcM (mean \u00b1 SEM,<jats:italic>n<\/jats:italic>= 5), respectively. The competition plot showed that ATP and ADP were hydrolyzed at the same active site on the enzyme. It may be postulated that the physiological role for this ecto\u2010enzyme cascade is to terminate the action of the co\u2010transmitter ATP, generating adenosine.<\/jats:p>","DOI":"10.1016\/j.cellbi.2005.10.027","type":"journal-article","created":{"date-parts":[[2006,2,10]],"date-time":"2006-02-10T12:29:58Z","timestamp":1139574598000},"page":"214-220","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Kinetic characterization of ATP diphosphohydrolase and 5\u2032\u2010nucleotidase activities in cells cultured from submandibular salivary glands of rats"],"prefix":"10.1002","volume":"30","author":[{"given":"Sandra Liana","family":"Henz","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cristiane 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