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Inhibitors were used to determine if the inhibitor profile of the ATPase was similar to that of a Ca<jats:sup>2+<\/jats:sup>-ATPase from parotid membranes identified previously as an ecto-ATPase. The Ca<jats:sup>2+<\/jats:sup>-ATPase of intact cells was insensitive to oligomycin (10 \u03bcg\/ml), N-ethylmaleimide (NEM) (0.1 m M), ruthenium red (0.1 m M), sodium azide (1 m M), and was inhibited approximately 22% by sodium orthovanadate (Na<jats:sub>3<\/jats:sub>VO<jats:sub>4<\/jats:sub>) (1 m M). This profile was similar to the Ca<jats:sup>2+<\/jats:sup>-ATPase of intact cells. Trifluoperazine (TFP) (0.1 m M) inhibited the enzyme in intact cells by approximately 32%. The nucleotide substrate specificity of the enzyme also reflected very closely the pattern seen in isolated membranes.<\/jats:p>","DOI":"10.1177\/10454411930040032201","type":"journal-article","created":{"date-parts":[[2017,1,6]],"date-time":"2017-01-06T00:46:03Z","timestamp":1483663563000},"page":"415-419","source":"Crossref","is-referenced-by-count":4,"title":["Localization and Characterization of a Parotid Ca2+-Dependent Ecto-ATPase"],"prefix":"10.1177","volume":"4","author":[{"given":"F.J.","family":"Dowd","sequence":"first","affiliation":[{"name":"Department of Pharmacology, School of Medicine, Creighton University, California at 24th Street, Omaha, NE 68178"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"L.S.","family":"Li","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, School of Medicine, Creighton University, California at 24th Street, Omaha, NE 68178"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"J.E.","family":"Campbell","sequence":"additional","affiliation":[{"name":"Department of Pharmacology, School of Medicine, Creighton University, California at 24th Street, Omaha, NE 68178"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"P.H.","family":"Cheung","sequence":"additional","affiliation":[{"name":"Department of Molecular Pathology, Box 89, M.D. Anderson Cancer Center, 1515 Holcombe Blvd, Houston, TX 77030"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[1993,4,1]]},"reference":[{"key":"atypb1","doi-asserted-by":"crossref","unstructured":"Ames, B.N.: Assay of Inorganic Phosphate, Total Phosphate and Phosphatases. In: Methods of Enzymology, Vol. 18, pp. 115-118. ( E. F. Neufeld and V. Ginsburg, Eds.) Academic Press, New York (1966).","DOI":"10.1016\/0076-6879(66)08014-5"},{"key":"atypb2","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(90)80264-J"},{"key":"atypb3","unstructured":"Cheung, P.H. and F.J. Dowd: A-Kinase Inhibits Rat Parotid Plasma Membrane Ca2+-ATPase. J. Dent. Res. 69:597(abs) (1990)."},{"key":"atypb4","unstructured":"Cheung, P.H. and F.J. Dowd: A Rat Parotid Membrane Ca2+-ATPase Resembles an Ecto-ATPase. J. Dent. Res. 70:373(abs) (1991)."},{"key":"atypb5","doi-asserted-by":"crossref","unstructured":"Depierre, J.W. and M.L. Karnovsky: Ectoenzymes of the Guinea Pig Polymorphonuclear Leukocyte. I. Evidence for an Ecto-Adenosine Monophosphatase, Adenosine Triphosphatase, and p-Nitrophenyl Phosphatase. J. Biol. Chem. 249:7111-7120 (1974).","DOI":"10.1016\/S0021-9258(19)42081-4"},{"key":"atypb6","doi-asserted-by":"crossref","unstructured":"Green, D.E., S., Mii, and P.M. 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