inosine-triphosphate and diazobenzenesulfonic-acid

inosine-triphosphate has been researched along with diazobenzenesulfonic-acid* in 1 studies

Other Studies

1 other study(ies) available for inosine-triphosphate and diazobenzenesulfonic-acid

Article	Year
Localization and characterization of a parotid Ca(2+)-dependent ecto-ATPase. Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists, 1993, Volume: 4, Issue:3-4 Parotid acini were isolated and tested to further establish the presence of ecto-ATPase in the intact cells. Inhibitors were used to determine if the inhibitor profile of the ATPase was similar to that of a Ca(2+)-ATPase from parotid membranes identified previously as an ecto-ATPase. The Ca(2+)-ATPase of intact cells was insensitive to oligomycin (10 micrograms/ml), N-ethylmaleimide (NEM) (0.1 mM), ruthenium red (0.1 mM), sodium azide (1 mM), and was inhibited approximately 22% by sodium orthovanadate (Na3VO4) (1 mM). This profile was similar to the Ca(2+)-ATPase of intact cells. Trifluoperazine (TFP) (0.1 mM) 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. Topics: Adenosine Triphosphatases; Animals; Azides; Calcium-Transporting ATPases; Cell Membrane; Cytidine Triphosphate; Diazonium Compounds; Ethylmaleimide; Guanosine Triphosphate; Inosine Triphosphate; Ouabain; Parotid Gland; Rats; Rats, Sprague-Dawley; Sodium Azide; Sulfanilic Acids; Trifluoperazine; Vanadates	1993

Article

Year

Localization and characterization of a parotid Ca(2+)-dependent ecto-ATPase.

Critical reviews in oral biology and medicine : an official publication of the American Association of Oral Biologists, 1993, Volume: 4, Issue:3-4

Parotid acini were isolated and tested to further establish the presence of ecto-ATPase in the intact cells. Inhibitors were used to determine if the inhibitor profile of the ATPase was similar to that of a Ca(2+)-ATPase from parotid membranes identified previously as an ecto-ATPase. The Ca(2+)-ATPase of intact cells was insensitive to oligomycin (10 micrograms/ml), N-ethylmaleimide (NEM) (0.1 mM), ruthenium red (0.1 mM), sodium azide (1 mM), and was inhibited approximately 22% by sodium orthovanadate (Na3VO4) (1 mM). This profile was similar to the Ca(2+)-ATPase of intact cells. Trifluoperazine (TFP) (0.1 mM) 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.

Topics: Adenosine Triphosphatases; Animals; Azides; Calcium-Transporting ATPases; Cell Membrane; Cytidine Triphosphate; Diazonium Compounds; Ethylmaleimide; Guanosine Triphosphate; Inosine Triphosphate; Ouabain; Parotid Gland; Rats; Rats, Sprague-Dawley; Sodium Azide; Sulfanilic Acids; Trifluoperazine; Vanadates

1993